https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Birgitte+ZeunerCAZypedia - User contributions [en-ca]2026-05-05T03:27:39ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=16831Glycoside Hydrolase Family 1512022-05-20T11:19:17Z<p>Birgitte Zeuner: </p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Casper Wilkens|Casper Wilkens]], [[User:David Teze|David Teze]], and [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
* [[Responsible Curator]]: [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] are bacterial enzymes presenting α-L-fucosidase activity ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (''p''NP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to [[GH42]] β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ''p''NP-β-D-Gal, ''p''NP-β-D-Glc, and ''p''NP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using ''p''NP-α-L-Fuc or CNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016 Teze2021</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
In the α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'', Glu235 was assigned as catalytic acid/base and Asp154 as catalytic nucleophile following a combination of mutational, structural, docking, and QM/MM studies <cite>Kovalova2022</cite>. Initially, both Asp9 and Asp154 were investigated as putative nucleophiles. However, docking studies combined with the fact that the variant D9N performed well in transglycosylation <cite>Teze2021</cite> indicated that the role of Asp9 is in substrate binding <cite>Kovalova2022</cite>.<br />
<br />
== Three-dimensional structures ==<br />
The first solved structure in GH151 was that of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus''. It revealed a tetrameric structure with active site complementation by His503 <cite>Kovalova2022</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Asp154 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First general acid/base residue identification: Glu235 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First 3-D structure: The 3-D structure of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
<br />
#Teze2021 pmid=33914359<br />
#Kovalova2022 pmid=35113503<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=16830Glycoside Hydrolase Family 1512022-05-20T11:18:08Z<p>Birgitte Zeuner: wording</p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Casper Wilkens|Casper Wilkens]], [[User:David Teze|David Teze]], and [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
* [[Responsible Curator]]: [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] are bacterial enzymes presenting α-L-fucosidase activity ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (''p''NP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to [[GH42]] β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ''p''NP-β-D-Gal, ''p''NP-β-D-Glc, and ''p''NP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using ''p''NP-α-L-Fuc or CNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016 Teze2021</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
In the α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'', Glu235 was assigned as catalytic acid/base and Asp154 as catalytic nucleophile following a combination of mutational, structural, docking, and QM/MM studies <cite>Kovalova2022</cite>. Initially, both Asp9 and Asp154 were investigated as putative nucleophiles. However, docking studies combined with the fact that the variant D9N performed well in transglycosylation <cite>Teze2021</cite> indicated that the role of Asp9 is in substrate binding <cite>Kovalova2022</cite>.<br />
<br />
== Three-dimensional structures ==<br />
The first solved structure in GH151 was that of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>. It revealed a tetrameric structure with active site complementation by His503.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Asp154 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First general acid/base residue identification: Glu235 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First 3-D structure: The 3-D structure of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
<br />
#Teze2021 pmid=33914359<br />
#Kovalova2022 pmid=35113503<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=16829Glycoside Hydrolase Family 1512022-05-20T11:17:02Z<p>Birgitte Zeuner: 3-D structure available</p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Casper Wilkens|Casper Wilkens]], [[User:David Teze|David Teze]], and [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
* [[Responsible Curator]]: [[User:Birgitte Zeuner|Birgitte Zeuner]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] are bacterial enzymes presenting α-L-fucosidase activity ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (''p''NP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to [[GH42]] β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ''p''NP-β-D-Gal, ''p''NP-β-D-Glc, and ''p''NP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using ''p''NP-α-L-Fuc or CNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016 Teze2021</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
In the α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'', Glu235 was assigned as catalytic acid/base and Asp154 as catalytic nucleophile following a combination of mutational, structural, docking, and QM/MM studies <cite>Kovalova2022</cite>. Initially, both Asp9 and Asp154 were investigated as putative nucleophiles. However, docking studies combined with the fact that the variant D9N performed well in transglycosylation <cite>Teze2021</cite> indicates that its role is in substrate binding <cite>Kovalova2022</cite>.<br />
<br />
== Three-dimensional structures ==<br />
The first solved structure in GH151 was that of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>. It revealed a tetrameric structure with active site complementation by His503.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Asp154 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First general acid/base residue identification: Glu235 in α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
;First 3-D structure: The 3-D structure of α-L-fucosidase isoenzyme 2 from ''Paenibacillus thiaminolyticus'' <cite>Kovalova2022</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
<br />
#Teze2021 pmid=33914359<br />
#Kovalova2022 pmid=35113503<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=16823User:Birgitte Zeuner2022-02-14T10:43:27Z<p>Birgitte Zeuner: /* Background */</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020a Zeuner2020c</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020a, Zeuner2020c</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017 Zeuner2020b</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
#Zeuner2020a pmid=32445980<br />
#Chung2017 pmid=29029078<br />
#Zeuner2016b pmid=26802542<br />
#Zeuner2020b pmid=32850731 <br />
#Zeuner2020c pmid=33217923<br />
#Teze2020 pmid=33914359<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=16822User:Birgitte Zeuner2022-02-14T10:42:30Z<p>Birgitte Zeuner: /* Selected papers */</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020a</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020a</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017 Zeuner2020b</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
#Zeuner2020a pmid=32445980<br />
#Chung2017 pmid=29029078<br />
#Zeuner2016b pmid=26802542<br />
#Zeuner2020b pmid=32850731 <br />
#Zeuner2020c pmid=33217923<br />
#Teze2020 pmid=33914359<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=16821User:Birgitte Zeuner2022-02-14T10:41:42Z<p>Birgitte Zeuner: /* Selected papers */</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020a</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020a</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017 Zeuner2020b</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
#Zeuner2020a pmid=32445980<br />
#Chung2017 pmid=29029078<br />
#Zeuner2016b pmid=26802542<br />
#Zeuner2020b pmid=32850731 <br />
#Zeuner2020c pmid=33217923<br />
<br />
#Teze2020 pmid=33914359<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=15802User:Birgitte Zeuner2020-08-26T11:50:23Z<p>Birgitte Zeuner: New reference</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020a</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020a</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017 Zeuner2020b</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
#Zeuner2020a pmid=32445980<br />
#Chung2017 pmid=29029078<br />
#Zeuner2016b pmid=26802542<br />
#Zeuner2020b Zeuner B, Thomsen TB, Stringer MA, Krogh KBRM, Meyer AS, Holck J. (2020) Comparative Characterization of Aspergillus Pectin Lyases by Discriminative Substrate Degradation Profiling. Front. Bioeng. Biotechnol. [https://doi.org/10.3389/fbioe.2020.00873 DOI: 10.3389/fbioe.2020.00873]<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=15549User:Birgitte Zeuner2020-07-07T09:14:51Z<p>Birgitte Zeuner: new pmid</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
#Zeuner2020 pmid=32445980<br />
#Chung2017 pmid=29029078<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15318Glycoside Hydrolase Family 1512020-06-13T17:32:38Z<p>Birgitte Zeuner: Curator Approved</p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] are bacterial enzymes presenting α-L-fucosidase activity ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (''p''NP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to [[GH42]] β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ''p''NP-β-D-Gal, ''p''NP-β-D-Glc, and ''p''NP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using ''p''NP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet solved.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15268Glycoside Hydrolase Family 1512020-06-12T08:48:02Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] are bacterial enzymes presenting α-L-fucosidase activity ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (''p''NP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to [[GH42]] β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ''p''NP-β-D-Gal, ''p''NP-β-D-Glc, and ''p''NP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using ''p''NP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet solved.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15210Glycoside Hydrolase Family 1512020-06-04T09:55:38Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on pNP-β-D-Gal, pNP-β-D-Glc, and pNP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet solved.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15209Glycoside Hydrolase Family 1512020-06-04T09:55:13Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on pNP-β-D-Gal, pNP-β-D-Glc, and pNP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15208Glycoside Hydrolase Family 1512020-06-04T09:41:46Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on pNP-β-D-Gal, pNP-β-D-Glc, and pNP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
#Lezyk2016 pmid=26800369<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15207Glycoside Hydrolase Family 1512020-06-04T09:39:41Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015</cite>. Sequence homology to β-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on pNP-β-D-Gal, pNP-β-D-Glc, and pNP-β-D-Lac, but none was observed <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15206Glycoside Hydrolase Family 1512020-06-04T09:36:34Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of [[GH151]] have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
The first characterized members of GH151 were perceived as members of [[GH29]] due to their α-L-fucosidase activity <cite>Sela2012 Lezyk2016</cite>. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 <cite>Sela2012 Lezyk2016</cite>. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created <cite>Benesova2015 Lezyk2016</cite>. Sequence homology to beta-galactosidase trimerization domains has been reported <cite>Sela2012 Lezyk2016</cite>. Consequently, one GH151 α-L-fucosidase was tested for activity on ...<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=15205Glycoside Hydrolase Family 1512020-06-04T09:14:30Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of GH151 have α-L-fucosidase activity (EC 3.2.1.51) <cite>Sela2012 Benesova2015 Lezyk2016</cite>. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) <cite>Benesova2015 Lezyk2016</cite> and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) <cite>Sela2012</cite>. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) <cite>Sela2012 Lezyk2016</cite>, but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal <cite>Sela2012</cite>. No activity was observed on fucosylated xyloglucan <cite>Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
The mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate <cite>Benesova2015 Lezyk2016</cite>, a retaining mechanism has been inferred.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues of GH151 are unknown.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structures have been solved for GH151.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=15017User:Birgitte Zeuner2020-05-28T03:19:55Z<p>Birgitte Zeuner: </p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557. [https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163. [https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365. [https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner B, Meyer AS (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res. 493, 108029. [https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=15016User:Birgitte Zeuner2020-05-28T03:19:20Z<p>Birgitte Zeuner: reference update</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner B, Meyer AS (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res. 493, 108029.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14883Glycoside Hydrolase Family 1512020-05-15T09:15:14Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Members of GH151 have α-L-fucosidase activity <cite>Sela2012 Benesova2015 Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14882Glycoside Hydrolase Family 1512020-05-15T09:14:55Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Authors]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Members of GH151 have α-L-fucosidase activity <cite>Sela2012 Benesova2015 Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14881Glycoside Hydrolase Family 1512020-05-15T09:14:08Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Members of GH151 have α-L-fucosidase activity <cite>Sela2012 Benesova2015 Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14880Glycoside Hydrolase Family 1512020-05-15T09:03:05Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Members of GH151 have α-L-fucosidase activity <cite>Sela2012 Benesova2015 Lezyk2016</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14879Glycoside Hydrolase Family 1512020-05-15T08:58:27Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
<br />
#Lezyk2016 pmid=26800369<br />
#Sela2012 pmid=22138995<br />
<br />
#Benesova2015 pmid=26013545<br />
<br />
<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_151&diff=14878Glycoside Hydrolase Family 1512020-05-15T08:46:07Z<p>Birgitte Zeuner: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Birgitte Zeuner^^^<br />
* [[Responsible Curator]]: ^^^Birgitte Zeuner^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH151'''<br />
|-<br />
|'''Clan''' <br />
|None<br />
|-<br />
|'''Mechanism'''<br />
|Retaining (inferred)<br />
|-<br />
|'''Active site residues'''<br />
|Not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH151.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH151]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=14877User:Birgitte Zeuner2020-05-15T07:59:43Z<p>Birgitte Zeuner: </p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here] and my contact details are [https://www.dtu.dk/english/service/phonebook/person?id=26799&tab=2&qt=dtupublicationquery here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner B, Meyer AS (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=14876User:Birgitte Zeuner2020-05-15T07:52:45Z<p>Birgitte Zeuner: </p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner B, Ståhlberg T, van Buu ON, Kunov-Kruse AJ, Riisager A, Meyer AS (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner B, González-Delgado I, Holck J, Morales G, López-Muñoz MJ, Segura Y, Meyer AS, Mikkelsen JD (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol J, Vuillemin M, Meyer AS, Zeuner B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner B, Meyer AS (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=14875User:Birgitte Zeuner2020-05-15T04:33:30Z<p>Birgitte Zeuner: </p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My ORCID is [https://orcid.org/0000-0002-8593-6742 here].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner, B., Ståhlberg, T., van Buu, O.N., Kunov-Kruse, A.J., Riisager, A., Meyer, A.S. (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner, B., González-Delgado, I., Holck, J., Morales, G., López-Muñoz, M.J., Segura, Y., Meyer, A.S., Mikkelsen, J.D. (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol, J., Vuillemin, M., Meyer, A.S., Zeuner, B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner, B., Meyer, A.S. (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=14874User:Birgitte Zeuner2020-05-15T04:31:25Z<p>Birgitte Zeuner: image and edit</p>
<hr />
<div>[[Image:BirgitteZeuner.jpg|150px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite>, [[GH20]] β-''N''-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner, B., Ståhlberg, T., van Buu, O.N., Kunov-Kruse, A.J., Riisager, A., Meyer, A.S. (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner, B., González-Delgado, I., Holck, J., Morales, G., López-Muñoz, M.J., Segura, Y., Meyer, A.S., Mikkelsen, J.D. (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol, J., Vuillemin, M., Meyer, A.S., Zeuner, B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner, B., Meyer, A.S. (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=File:BirgitteZeuner.jpg&diff=14873File:BirgitteZeuner.jpg2020-05-15T04:28:40Z<p>Birgitte Zeuner: </p>
<hr />
<div></div>Birgitte Zeunerhttps://www.cazypedia.org/index.php?title=User:Birgitte_Zeuner&diff=14872User:Birgitte Zeuner2020-05-15T04:09:46Z<p>Birgitte Zeuner: Content</p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
'''Assistant Professor''' at the [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark].<br />
<br />
== Background ==<br />
<br />
I obtained an MSc degree in Biotechnology at [https://www.kt.dtu.dk Department of Chemical and Biochemical Engineering], [https://www.dtu.dk Technical University of Denmark] in 2009. I continued my PhD studies there under the supervision of Anne S. Meyer, where I worked with [[CE1]] feruloyl esterases to catalyze transesterification in ionic liquids <cite>Zeuner2011 Zeuner2012</cite>, as well as with [[GH33]] sialidases for transsialylation <cite>Zeuner2014a Zeuner2014b</cite>. Starting from solvent engineering and reaction design to improve enzyme-catalysed synthesis, my work has since evolved to include protein engineering and enzyme discovery. My post doc studies included a lot of carbohydrate analysis (HPAEC-PAD) and work on [[GH33]] sialidases <cite>Zeuner2016a Nordvang2016 Zeuner2017</cite>, [[GH29]] α-L-fucosidases <cite>Zeuner2018a Zeuner2018b Zeuner2020</cite> , [[GH20]] β-N-acetylhexosaminidases <cite>Nyffenegger2015 Jamek2018</cite>, and other GH families <cite>Zeuner2016b</cite> for transglycosylation to yield human milk oligosaccharide structures. In 2018, I was appointed Assistant Professor in Enzyme Technology for Oligosaccharide Synthesis at [https://www.bioengineering.dtu.dk/english Department of Biotechnology and Biomedicine], [https://www.dtu.dk Technical University of Denmark]. My current work focuses on transglycosylation <cite>Zeuner2014c, Zeuner2019, Muschiol2020, Zeuner2020</cite>. As GH-catalysed synthesis is not always a walk in the park, I sometimes spend time off from that to deal with targeted carbohydrate breakdown using [[PL1]] pectin lyases <cite>Chung2017</cite>.<br />
<br />
== Selected papers ==<br />
<br />
<biblio><br />
<br />
#Zeuner2011 Zeuner, B., Ståhlberg, T., van Buu, O.N., Kunov-Kruse, A.J., Riisager, A., Meyer, A.S. (2011) Dependency of the hydrogen bonding capacity of the solvent anion on the thermal stability of feruloyl esterases in ionic liquid systems. Green Chem. 13, 1550-1557.[https://doi.org/10.1039/C1GC15115K DOI: 10.1039/C1GC15115K]<br />
#Zeuner2012 pmid=22154740<br />
#Zeuner2014a pmid=24411449<br />
#Zeuner2014b pmid=24563319<br />
#Zeuner2016a pmid=26672447<br />
#Nordvang2016 pmid=27367145<br />
#Zeuner2017 Zeuner, B., González-Delgado, I., Holck, J., Morales, G., López-Muñoz, M.J., Segura, Y., Meyer, A.S., Mikkelsen, J.D. (2017) Characterization and immobilization of engineered sialidases from Trypanosoma rangeli for transsialylation. AIMS Mol. Sci. 4(2), 140-163.[https://doi.org/10.3934/molsci.2017.2.140 DOI: 10.3934/molsci.2017.2.140]<br />
#Muschiol2020 Muschiol, J., Vuillemin, M., Meyer, A.S., Zeuner, B. (2020) β-N-Acetylhexosaminidases for carbohydrate synthesis via trans-glycosylation. Catalysts 10, 365.[https://doi.org/10.3390/catal10040365 DOI: 10.3390/catal10040365]<br />
#Jamek2018 pmid=29911342<br />
#Nyffenegger2015 pmid=25843303<br />
#Zeuner2019 pmid=31141914<br />
#Zeuner2014c pmid=25208138<br />
<br />
#Zeuner2018a pmid=29221760<br />
#Zeuner2018b pmid=29859601<br />
<br />
#Zeuner2020 Zeuner, B., Meyer, A.S. (2020) Enzymatic transfucosylation for synthesis of human milk oligosaccharides. Carbohydr. Res.[https://doi.org/10.1016/j.carres.2020.108029 DOI: 10.1016/j.carres.2020.108029]<br />
<br />
#Chung2017 pmid=29029078<br />
<br />
#Zeuner2016b pmid=26802542<br />
<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Zeuner,Birgitte]]</div>Birgitte Zeuner