CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 164

2020-04-02T21:31:29Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


[[Image:BS164_AB.png|thumb|right|400px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]
== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
''Bs''164 β-mannosidase is a [[retaining]] enzyme, as first shown by NMR <cite>Armstrong2020</cite>, and follows the [[classical Koshland double-displacement mechanism]].

== Catalytic Residues ==
The catalytic nucleophile of ''Bs''164 was identified as glutamate 297 through mutational analysis<cite>Armstrong2020</cite>. A structural complex with 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-mannopyranoside showed a covalent attachment of the inhibitor to glutamate 297, reinforcing the assignment of Glu297 as the catalytic nucleophile. The acid/base residue, Glu160 is positioned to perform ''anti''-protonation of the leaving group, typical of clan GH-A glycoside hydrolases. This residue forms hydrogen bonding interactions with both the endocyclic nitrogen in noeuromycin and imidazole nitrogen in mannoimidazole. Complete loss of activity by the E160Q variant confirmed the assignment of Glu160 as the acid/base residue<cite>Armstrong2020</cite>.

== Three-dimensional structures ==
To date only the structure of ''Bs''164 has been solved. ''Bs''164 was solved using multi-wavelength anomalous diffraction of a seleno-methionine labeled protein<cite>Armstrong2020</cite>. The structure of ''Bs''164 has been solved in an uncomplexed state and in complex with mannoimidazole, noeuromycin and 2-deoxy-2-fluoromannose. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)<sub>8</sub> barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). The catalytic residues are present on strands 4 (acid/base) and 7
(nucleophile) of the (β/α)<sub>8</sub> barrel indicating that GH164 belongs to clan GH-A glycoside hydrolases. This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.

== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416
#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T21:30:27Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


[[Image:BS164_AB.png|thumb|right|400px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]
== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
''Bs''164 β-mannosidase is a [[retaining]] enzyme, as first shown by NMR <cite>Armstrong2020</cite>, and follows the [[classical Koshland double-displacement mechanism]].

== Catalytic Residues ==
The catalytic nucleophile of ''Bs''164 was identified as glutamate 297 through mutational analysis<cite>Armstrong2020</cite>. A structural complex with 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-mannopyranoside showed a covalent attachment of the inhibitor to glutamate 297, reinforcing the assignment of Glu297 as the catalytic nucleophile. The acid/base residue, Glu160 is positioned to perform ''anti''-protonation of the leaving group, typical of clan GH-A glycoside hydrolases. This residue forms hydrogen bonding interactions with both the endocyclic nitrogen in noeuromycin and imidazole nitrogen in mannoimidazole. Complete loss of activity by the E160Q variant confirmed the assignment of Glu160 as the acid/base residue<cite>Armstrong2020</cite>.

== Three-dimensional structures ==
To date only the structure of ''Bs''164 has been solved. ''Bs''164 was solved using multi-wavelength anomalous diffraction of a seleno-methionine labeled protein<cite>Armstrong2020</cite>. The structure of ''Bs''164 has been solved in an uncomplexed state and in complex with mannoimidazole, noeuromycin and 2-deoxy-2-fluoromannose. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)<sub>8</sub> barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). The catalytic residues are present on strands 4 (acid/base) and 7
(nucleophile) of the (β/α)<sub>8</sub> barrel indicating that the GH164 belongs to clan GH-A glycoside hydrolases. This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.

== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416
#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T21:24:07Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
''Bs''164 β-mannosidase is a [[retaining]] enzyme, as first shown by NMR <cite>Armstrong2020</cite>, and follows the [[classical Koshland double-displacement mechanism]].

== Catalytic Residues ==
The catalytic nucleophile of ''Bs''164 was identified as glutamate 297 through mutational analysis<cite>Armstrong2020</cite>. A structural complex with 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-mannopyranoside showed a covalent attachment of the inhibitor to glutamate 297, reinforcing the assignment of Glu297 as the catalytic nucleophile. The acid/base residue, Glu160 is positioned to perform ''anti''-protonation of the leaving group, typical of clan GH-A glycoside hydrolases. This residue forms hydrogen bonding interactions with both the endocyclic nitrogen in noeuromycin and imidazole nitrogen in mannoimidazole. Complete loss of activity by the E160Q variant confirmed the assignment of Glu160 as the acid/base residue<cite>Armstrong2020</cite>.

== Three-dimensional structures ==
[[Image:BS164_AB.png|thumb|right|400px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]

To date only the structure of ''Bs''164 has been solved. ''Bs''164 was solved using multi-wavelength anomalous diffraction of a seleno-methionine labeled protein<cite>Armstrong2020</cite>. The structure of ''Bs''164 has been solved in both the free and in complex with mannoimidazole, noeuromycin or 2-deoxy-2-fluoromannose. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)<sub>8</sub> barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.
== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416
#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T21:21:04Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
''Bs''164 β-mannosidase is a [[retaining]] enzyme, as first shown by NMR <cite>Armstrong2020</cite>, and follows the [[classical Koshland double-displacement mechanism]].

== Catalytic Residues ==
The catalytic nucleophile of ''Bs''164 was identified as glutamate 297 through mutational analysis<cite>Armstrong2020</cite>. Structural complexes with 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-mannopyranoside also showed a covalent attachment of the inhibitor to glutamate 297. The acid/base residue, Glu160 is positioned to perform anti-protonation of the leaving group, typical of clan GH-A glycoside hydrolases. This residue forms hydrogen bonding interactions with both the endocyclic nitrogen in noeuromycin and imidazole nitrogen in mannoimidazole. Complete loss of activity by the E160Q variant confirmed the assignment of Glu160 as the acid/base residue<cite>Armstrong2020</cite>.

== Three-dimensional structures ==
[[Image:BS164_AB.png|thumb|right|400px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]

To date only the structure of ''Bs''164 has been solved. ''Bs''164 was solved using multi-wavelength anomalous diffraction of a seleno-methionine labeled protein<cite>Armstrong2020</cite>. The structure of ''Bs''164 has been solved in both the free and in complex with mannoimidazole, noeuromycin or 2-deoxy-2-fluoromannose. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)<sub>8</sub> barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.
== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416
#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T20:55:45Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
Content is to be added here.

== Three-dimensional structures ==
[[Image:BS164_AB.png|thumb|right|450px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]

To date only the structure of Bacteroidetes salyersiae β-mannosidase (Bs164) has been solved. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)8 barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.

== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416

#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T20:54:37Z

Zachary Armstrong:

{{UnderConstruction}}
* [[Author]]: ^^^Zachary Armstrong^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH164'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH164.html
|}
</div>


== Substrate specificities ==
The defining member of [[glycoside hydrolase]] family 164, a β-mannosidase from ''Bacteroidetes salyersiae'' (''Bs''164, GenbankID: EIY59668.1), was identified initially identified through rational bioinformatic selection of enzyme targets <cite>Helbert2019</cite>. Although ''Bs''164 was initially reported as an α-mannosidase, subsequent detailed biochemical characterization and structure determination revealed that was instead a β-mannosidase <cite>Armstrong2020</cite>. This enzyme is an exo-acting and is capable of cleaving mannooligos and β-mannosides<cite>Armstrong2020</cite>.

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
Content is to be added here.

== Three-dimensional structures ==
To date only the structure of Bacteroidetes salyersiae β-mannosidase (Bs164) has been solved. Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)8 barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002</cite>, but is previously unseen for β-mannosidases.

[[Image:BS164_AB.png|thumb|right|450px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']]
== Family Firsts ==
;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
== References ==
<biblio>
#Helbert2019 pmid=30850540
#Hidaka2002 pmid=12215416

#Armstrong2020 pmid=31871050

</biblio>

[[Category:Glycoside Hydrolase Families|GH164]]

Glycoside Hydrolase Family 164

2020-04-02T20:29:04Z

Zachary Armstrong:

Glycoside Hydrolase Family 164

2020-04-02T18:12:42Z

Zachary Armstrong:

Glycoside Hydrolase Family 164

2020-04-02T18:09:45Z

Zachary Armstrong:

Glycoside Hydrolase Family 164

2020-04-02T18:08:38Z

Zachary Armstrong:

Glycoside Hydrolase Family 164

2020-04-02T17:47:29Z

Zachary Armstrong:

File:BS164 AB.png

2020-04-02T17:35:55Z

Zachary Armstrong: Zachary Armstrong uploaded a new version of File:BS164 AB.png

File:BS164 AB.png

2020-04-02T17:34:06Z

Zachary Armstrong:

File:BS164 AB.gif

2020-04-02T17:32:34Z

Zachary Armstrong:

Glycoside Hydrolase Family 164

2020-04-02T16:18:16Z

Zachary Armstrong:

User:Zachary Armstrong

2020-04-02T15:58:05Z

Zachary Armstrong:

[[Image:Z_Armstrong.png|200px|right]]

Dr. Zachary Armstrong, a native of Iqaluit, Nunavut, obtained his B.Sc. — majoring in chemistry and biochemistry — from the [https://www.ubc.ca/ University of British Columbia]. His final year project, performed under the guidance of Professor [[User:Steve Withers|Steve Withers]], focused on the creation of a [[GH11]] thioglycoligase <cite>Armstrong2010</cite>. He completed his PhD at the University of British Columbia, co-supervised by Professors Steve Withers and [http://hallam.microbiology.ubc.ca/ Steven J. Hallam]. This work focused on the identification of glycoside hydrolases from metagenomic sources — including the beaver gut<cite>Armstrong2018</cite>,a mining bioreactor<cite>Armstrong2013</cite> and soils<cite>Armstrong2019mSys</cite>— and the engineering of glycosynthases from metagenomes and synthetic gene libraries<cite>Armstrong2019Acs</cite>. In 2018 he joined the group of [[User:Gideon Davies|Gideon Davies]] in the [https://www.york.ac.uk/chemistry/research/ysbl/ York Structural Biology Laboratories] at the [https://www.york.ac.uk/ University of York] as a postdoctoral research associate. His current work focuses on mechanism-based inhibitors and activity-based protein profiling of human carbohydrate processing enzymes.

He has determined the crystal structure of :

* [[GH164]] ''Bacteroides salyersiae'' beta-mannosidase <cite>Armstrong2019JBC</cite>

----

<biblio>
#Armstrong2010 pmid=20112321
#Armstrong2018 pmid=30013164
#Armstrong2019mSys pmid=31164449
#Armstrong2013 pmid=23906845
#Armstrong2019Acs Armstrong Z, Liu F, Chen H-M, Hallam SJ, Withers SG. (2019) Systematic Screening of Synthetic Gene-Encoded Enzymes for Synthesis of Modified Glycosides. ''ACS Catal''. 53, 689-98. | [https://doi.org/10.1021/acscatal.8b05179 DOI: 10.1021/acscatal.8b05179]
#Armstrong2019JBC pmid=31871050

</biblio>

[[Category:Contributors|Armstrong,Zachary]]

User:Zachary Armstrong

2020-04-02T14:20:00Z

Zachary Armstrong:

[[Image:Z_Armstrong.png|200px|right]]

Dr. Zachary Armstrong, a native of Iqaluit, Nunavut, obtained his B.Sc. — majoring in chemistry and biochemistry — from the [https://www.ubc.ca/ University of British Columbia]. His final year project, performed under the guidance of Professor [[User:Steve Withers|Steve Withers]], focused on the creation of a [[GH11]] thioglycoligase <cite>Armstrong2010</cite>. He completed his PhD at the University of British Columbia, co-supervised by Professors Steven Withers and [http://hallam.microbiology.ubc.ca/ Stephen J. Hallam]. This work focused on the identification of glycoside hydrolases from metagenomic sources — including the beaver gut<cite>Armstrong2018</cite>,a mining bioreactor<cite>Armstrong2013</cite> and soils<cite>Armstrong2019mSys</cite>— and the engineering of glycosynthases from a metagenomes and synthetic gene libraries<cite>Armstrong2019Acs</cite>. In 2018 he joined the group of [[User:Gideon Davies|Gideon Davies]] in the [https://www.york.ac.uk/chemistry/research/ysbl/ York Structural Biology Laboratories] at the [https://www.york.ac.uk/ University of York] as a postdoctoral research associate. His current work focuses on mechanism-based inhibitors and activity-based protein profiling of human carbohydrate processing enzymes.

He has determined the crystal structure of :

* [[GH164]] ''Bacteroides salyersiae'' beta-mannosidase <cite>Armstrong2019JBC</cite>

----

<biblio>
#Armstrong2010 pmid=20112321
#Armstrong2018 pmid=30013164

#Armstrong2019mSys pmid=31164449
#Armstrong2013 pmid=23906845

#Armstrong2019Acs doi=10.1021/acscatal.8b05179

#Armstrong2019JBC pmid=31871050

</biblio>

[[Category:Contributors|Armstrong,Zachary]]

User:Zachary Armstrong

2020-04-02T14:13:30Z

Zachary Armstrong:

[[Image:Z_Armstrong.png|200px|right]]

Dr. Zachary Armstrong, a native of Iqaluit, Nunavut, obtained his B.Sc. — majoring in chemistry and biochemistry — from the [https://www.ubc.ca/ University of British Columbia]. His final year project, performed under the guidance of Professor [[User:Steve Withers|Steve Withers]], focused on the creation of a [[GH11]] thioglycoligase <cite>Armstrong2010</cite>. He completed his PhD at the University of British Columbia, co-supervised by Professors Steven Withers and Stephen J. Hallam. This work focused on the identification of glycoside hydrolases from metagenomic sources — including the beaver gut<cite>Armstrong2018</cite>,a mining bioreactor<cite>Armstrong2013</cite> and soils<cite>Armstrong2019mSys</cite>— and the engineering of glycosynthases from a metagenomes and synthetic gene libraries (ref). In 2018 he joined the group of [[User:Gideon Davies|Gideon Davies]] in the [https://www.york.ac.uk/chemistry/research/ysbl/ York Structural Biology Laboratories] at the [https://www.york.ac.uk/ University of York] as a postdoctoral research associate. His current work focuses on mechanism-based inhibitors and activity-based protein profiling of human carbohydrate processing enzymes.

He has determined the crystal structure of :

* [[GH164]] ''Bacteroides salyersiae'' beta-mannosidase <cite> </cite>

----

<biblio>
#Armstrong2010 pmid=20112321
#Armstrong2018 pmid=30013164

#Armstrong2019mSys pmid=31164449
#Armstrong2013 pmid=23906845
</biblio>

[[Category:Contributors|Armstrong,Zachary]]

File:Z Armstrong.png

2020-04-02T14:07:35Z

Zachary Armstrong:

User:Zachary Armstrong

2020-04-02T14:00:55Z

Zachary Armstrong:

[[Image:Blank_user-200px.png|200px|right]]

Dr. Zachary Armstrong, a native of Iqaluit, Nunavut, obtained his B.Sc. — majoring in chemistry and biochemistry — from the University of British Columbia (https://www.ubc.ca/). His final year project, performed under the guidance of [[User:Steve Withers|Steve Withers]], focused on the creation of a [[GH11]] thioglycoligase <cite>Armstrong2010</cite>. He completed his PhD at the University of British Columbia, co-supervised by Professor Steven Withers and Stephen Hallam. This work focused on the identification of glycoside hydrolases from metagenomic sources — including the beaver gut<cite>Armstrong2018</cite>,a mining bioreactor<cite>Armstrong2013</cite> and soils<cite>Armstrong2019mSys</cite>— and the engineering of glycosynthases from a metagenomes and synthetic gene libraries (ref). In 2018 he joined the group of [[User:Gideon Davies|Gideon Davies]] in the York Structural Biology Laboratories (https://www.york.ac.uk/chemistry/research/ysbl/ ) at the University of York (https://www.york.ac.uk/) as a postdoctoral research associate. His current work focuses on mechanism-based inhibitors and activity-based protein profiling of human carbohydrate processing enzymes.

He has determined the crystal structure of :

* [[GH164]] ''Bacteroides salyersiae'' beta-mannosidase <cite> </cite>

* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.
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----

<biblio>
#Armstrong2010 pmid=20112321
#Armstrong2018 pmid=30013164

#Armstrong2019mSys pmid=31164449
#Armstrong2013 pmid=23906845
</biblio>

[[Category:Contributors|Armstrong,Zachary]]