CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 30

2010-11-05T22:15:14Z

Franz St. John:

{{CuratorApproved}}
* [[Author]]: [[User:Brian Rempel|Brian Rempel]]
* [[Responsible Curator]]: [[User:Steve Withers|Stephen Withers]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 30'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH30.html
|}
</div>

==Family Classification==
[[GH30]] classification has recently been revised <cite>stjohn2010</cite>. As had been suggested in several reports with respect to glucuronoxylan xylanohydrolases (previously of [[GH5]]) <cite>brumshtein2006,haegeman2009,keen1996,larson2003, mitreva-dautova2006</cite>, these enzymes through sequence analysis appear to be more like enzymes of [[GH30]]. In consideration of these observation the new classification employed phylogenetics, primary amino acid sequence and structure analysis to show that the glucuronoxylan xylanohydrolase in question as well as several other enzyme groups classified as [[GH5]] enzymes actually are [[GH30] enzymes.

==Substrate Specificities==
This family contains [[glycoside hydrolases]] with three known enzyme activities: β-glucosylceramidase, β-1,6-glucanase, and β-xylosidase. This family currently contains enzymes from only bacteria and eukaryotes. The best-studied enzyme is human β-glucocerebrosidase whose deficiency causes Gauchers disease <cite>grabowski2008</cite>. This enzyme is responsible for hydrolyzing the β-glucoside from the glycolipid glucosylceramide.

==Kinetics and Mechanism==
Family GH30 enzymes are [[retaining]] enzymes. Although this has never been formally demonstrated experimentally through NMR analysis of the initially formed sugar product, covalent trapping of the [[catalytic nucleophile]] (described below) conclusively demonstrates that these enzymes follow the classic [[Koshland double-displacement mechanism]]. The β-glucosylceramidases require an activator protein and negatively charged phospholipids for optimal activity, <cite>grabowski1990</cite> although the role of these activators is still not entirely clear. Neither the β-1,6-glucanases <cite>oyama2002</cite> nor the β-xylosidases <cite>brunner2002</cite> appear to require any activators.

==Catalytic Residues==
The [[catalytic nucleophile]] was first identified in human β-glucocerebrosidase as Glu340 in the sequence FAS<u>'''E'''</u>A by trapping of the 2-deoxy-2-fluoro-glucosyl-enzyme [[intermediate]] and subsequent peptide mapping by LC/MS-MS <cite>miao1994</cite>. The [[catalytic nucleophile]] had been previously been mistakenly identified as Asp443 using a tritiated bromoconduritol epoxide <cite>dinur1986, legler1990</cite>, although subsequent kinetic analyses of site-directed mutants of Asp443 were not consistent with its role as the [[catalytic nucleophile]] <cite>grace1994</cite>. The [[general acid/base]] residue of human β-glucoerebrosidase is predicted to be Glu-274 <cite>durand1997</cite>. While this identification has not been experimentally verified through analysis of variant proteins created by mutation of that site, it is consistent with structural studies (below).

==Three-Dimensional Structures==
The three-dimensional structure of human β-glucocerebrosidase was first solved in 2003 <cite>dvir2003</cite>, and since then several different structures of this enzyme have been reported (reviewed in <cite>kacher2008</cite>). GH30 enzymes are members of the GHA clan fold, consistent with the classic (α/β)<sub>8</sub> TIM barrel fold with the two key active site glutamic acids located at the C-terminal ends of β-strands 4 (acid/base) and 7 (nucleophile) <cite>henrissat1995</cite>.

==Family Firsts==

;'''First [[catalytic nucleophile]] identification'''
:Human β-glucocerebrosidase by 2-fluoroglucose labelling <cite>#1</cite>
;'''First 3-D structure of a GH30 enzyme'''
:Human β-glucocerebrosidase <cite>#2</cite>

==References==
<biblio>
# brumshtein2006 pmid=17139081
# haegeman2009 pmid=19400841
# keen1996 pmid=8810080
# larson2003 pmid=12859186
# mitreva-dautova2006 pmid=16673939
# stjohn2010 pmid=20932833
# grabowski2008 pmid=19094956
# grabowski1990 pmid=2127241
# oyama2002 pmid=12162562
# brunner2002 pmid=11909624
# miao1994 pmid=7908905
# dinur1986 pmid=3456607
# legler1990 pmid=2077872
# grace1994 pmid=8294487
# durand1997 pmid=9134434
# dvir2003 pmid=12792654
# kacher2008 pmid=18783340
# henrissat1995 pmid=7624375
</biblio>

[[Category:Glycoside Hydrolase Families|GH030]]

Glycoside Hydrolase Family 30

2010-11-05T22:08:00Z

Franz St. John:

{{CuratorApproved}}
* [[Author]]: [[User:Brian Rempel|Brian Rempel]]
* [[Responsible Curator]]: [[User:Steve Withers|Stephen Withers]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 30'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH30.html
|}
</div>

==Family Classification==
[[GH30]] classification has recently been revised <cite>stjohn2010</cite>. As had been suggested in several reports with respect to glucuronoxylan xylanohydrolases (previously of [[GH5]])<cite>brumshtein2006,haegeman2009,keen1996,larson2003, mitreva-dautova2006</cite>, these enzymes through sequence analysis appear to be more like enzymes of [[GH30]].

==Substrate Specificities==
This family contains [[glycoside hydrolases]] with three known enzyme activities: β-glucosylceramidase, β-1,6-glucanase, and β-xylosidase. This family currently contains enzymes from only bacteria and eukaryotes. The best-studied enzyme is human β-glucocerebrosidase whose deficiency causes Gauchers disease <cite>grabowski2008</cite>. This enzyme is responsible for hydrolyzing the β-glucoside from the glycolipid glucosylceramide.

==Kinetics and Mechanism==
Family GH30 enzymes are [[retaining]] enzymes. Although this has never been formally demonstrated experimentally through NMR analysis of the initially formed sugar product, covalent trapping of the [[catalytic nucleophile]] (described below) conclusively demonstrates that these enzymes follow the classic [[Koshland double-displacement mechanism]]. The β-glucosylceramidases require an activator protein and negatively charged phospholipids for optimal activity, <cite>grabowski1990</cite> although the role of these activators is still not entirely clear. Neither the β-1,6-glucanases <cite>oyama2002</cite> nor the β-xylosidases <cite>brunner2002</cite> appear to require any activators.

==Catalytic Residues==
The [[catalytic nucleophile]] was first identified in human β-glucocerebrosidase as Glu340 in the sequence FAS<u>'''E'''</u>A by trapping of the 2-deoxy-2-fluoro-glucosyl-enzyme [[intermediate]] and subsequent peptide mapping by LC/MS-MS <cite>miao1994</cite>. The [[catalytic nucleophile]] had been previously been mistakenly identified as Asp443 using a tritiated bromoconduritol epoxide <cite>dinur1986, legler1990</cite>, although subsequent kinetic analyses of site-directed mutants of Asp443 were not consistent with its role as the [[catalytic nucleophile]] <cite>grace1994</cite>. The [[general acid/base]] residue of human β-glucoerebrosidase is predicted to be Glu-274 <cite>durand1997</cite>. While this identification has not been experimentally verified through analysis of variant proteins created by mutation of that site, it is consistent with structural studies (below).

==Three-Dimensional Structures==
The three-dimensional structure of human β-glucocerebrosidase was first solved in 2003 <cite>dvir2003</cite>, and since then several different structures of this enzyme have been reported (reviewed in <cite>kacher2008</cite>). GH30 enzymes are members of the GHA clan fold, consistent with the classic (α/β)<sub>8</sub> TIM barrel fold with the two key active site glutamic acids located at the C-terminal ends of β-strands 4 (acid/base) and 7 (nucleophile) <cite>henrissat1995</cite>.

==Family Firsts==

;'''First [[catalytic nucleophile]] identification'''
:Human β-glucocerebrosidase by 2-fluoroglucose labelling <cite>#1</cite>
;'''First 3-D structure of a GH30 enzyme'''
:Human β-glucocerebrosidase <cite>#2</cite>

==References==
<biblio>
# brumshtein2006 pmid=17139081
# haegeman2009 pmid=19400841
# keen1996 pmid=8810080
# larson2003 pmid=12859186
# mitreva-dautova2006 pmid=16673939
# stjohn2010 pmid=20932833
# grabowski2008 pmid=19094956
# grabowski1990 pmid=2127241
# oyama2002 pmid=12162562
# brunner2002 pmid=11909624
# miao1994 pmid=7908905
# dinur1986 pmid=3456607
# legler1990 pmid=2077872
# grace1994 pmid=8294487
# durand1997 pmid=9134434
# dvir2003 pmid=12792654
# kacher2008 pmid=18783340
# henrissat1995 pmid=7624375
</biblio>

[[Category:Glycoside Hydrolase Families|GH030]]

Glycoside Hydrolase Family 30

2010-11-05T21:27:29Z

Franz St. John:

{{CuratorApproved}}
* [[Author]]: [[User:Brian Rempel|Brian Rempel]]
* [[Responsible Curator]]: [[User:Steve Withers|Stephen Withers]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 30'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH30.html
|}
</div>

==Family Classification==
[[GH30]] classification has recently been revised <cite>stjohn2010</cite>. It has been suggested previously is several reports that with respect to [[GH5]] glucuronoxylan xylanohydrolases

==Substrate Specificities==
This family contains [[glycoside hydrolases]] with three known enzyme activities: β-glucosylceramidase, β-1,6-glucanase, and β-xylosidase. This family currently contains enzymes from only bacteria and eukaryotes. The best-studied enzyme is human β-glucocerebrosidase whose deficiency causes Gauchers disease <cite>grabowski2008</cite>. This enzyme is responsible for hydrolyzing the β-glucoside from the glycolipid glucosylceramide.

==Kinetics and Mechanism==
Family GH30 enzymes are [[retaining]] enzymes. Although this has never been formally demonstrated experimentally through NMR analysis of the initially formed sugar product, covalent trapping of the [[catalytic nucleophile]] (described below) conclusively demonstrates that these enzymes follow the classic [[Koshland double-displacement mechanism]]. The β-glucosylceramidases require an activator protein and negatively charged phospholipids for optimal activity, <cite>grabowski1990</cite> although the role of these activators is still not entirely clear. Neither the β-1,6-glucanases <cite>oyama2002</cite> nor the β-xylosidases <cite>brunner2002</cite> appear to require any activators.

==Catalytic Residues==
The [[catalytic nucleophile]] was first identified in human β-glucocerebrosidase as Glu340 in the sequence FAS<u>'''E'''</u>A by trapping of the 2-deoxy-2-fluoro-glucosyl-enzyme [[intermediate]] and subsequent peptide mapping by LC/MS-MS <cite>miao1994</cite>. The [[catalytic nucleophile]] had been previously been mistakenly identified as Asp443 using a tritiated bromoconduritol epoxide <cite>dinur1986, legler1990</cite>, although subsequent kinetic analyses of site-directed mutants of Asp443 were not consistent with its role as the [[catalytic nucleophile]] <cite>grace1994</cite>. The [[general acid/base]] residue of human β-glucoerebrosidase is predicted to be Glu-274 <cite>durand1997</cite>. While this identification has not been experimentally verified through analysis of variant proteins created by mutation of that site, it is consistent with structural studies (below).

==Three-Dimensional Structures==
The three-dimensional structure of human β-glucocerebrosidase was first solved in 2003 <cite>dvir2003</cite>, and since then several different structures of this enzyme have been reported (reviewed in <cite>kacher2008</cite>). GH30 enzymes are members of the GHA clan fold, consistent with the classic (α/β)<sub>8</sub> TIM barrel fold with the two key active site glutamic acids located at the C-terminal ends of β-strands 4 (acid/base) and 7 (nucleophile) <cite>henrissat1995</cite>.

==Family Firsts==

;'''First [[catalytic nucleophile]] identification'''
:Human β-glucocerebrosidase by 2-fluoroglucose labelling <cite>#1</cite>
;'''First 3-D structure of a GH30 enzyme'''
:Human β-glucocerebrosidase <cite>#2</cite>

==References==
<biblio>
# stjohn2010 pmid=20932833
# grabowski2008 pmid=19094956
# grabowski1990 pmid=2127241
# oyama2002 pmid=12162562
# brunner2002 pmid=11909624
# miao1994 pmid=7908905
# dinur1986 pmid=3456607
# legler1990 pmid=2077872
# grace1994 pmid=8294487
# durand1997 pmid=9134434
# dvir2003 pmid=12792654
# kacher2008 pmid=18783340
# henrissat1995 pmid=7624375
</biblio>

[[Category:Glycoside Hydrolase Families|GH030]]

Glycoside Hydrolase Family 30

2010-11-05T21:08:30Z

Franz St. John:

{{CuratorApproved}}
* [[Author]]: [[User:Brian Rempel|Brian Rempel]]
* [[Responsible Curator]]: [[User:Steve Withers|Stephen Withers]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 30'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH30.html
|}
</div>

==Substrate specificities==
This family contains [[glycoside hydrolases]] with three known enzyme activities: β-glucosylceramidase, β-1,6-glucanase, and β-xylosidase. This family currently contains enzymes from only bacteria and eukaryotes. The best-studied enzyme is human β-glucocerebrosidase whose deficiency causes Gauchers disease <cite>grabowski2008</cite>. This enzyme is responsible for hydrolyzing the β-glucoside from the glycolipid glucosylceramide.

==Kinetics and Mechanism==
Family GH30 enzymes are [[retaining]] enzymes. Although this has never been formally demonstrated experimentally through NMR analysis of the initially formed sugar product, covalent trapping of the [[catalytic nucleophile]] (described below) conclusively demonstrates that these enzymes follow the classic [[Koshland double-displacement mechanism]]. The β-glucosylceramidases require an activator protein and negatively charged phospholipids for optimal activity, <cite>grabowski1990</cite> although the role of these activators is still not entirely clear. Neither the β-1,6-glucanases <cite>oyama2002</cite> nor the β-xylosidases <cite>brunner2002</cite> appear to require any activators.

==Catalytic Residues==
The [[catalytic nucleophile]] was first identified in human β-glucocerebrosidase as Glu340 in the sequence FAS<u>'''E'''</u>A by trapping of the 2-deoxy-2-fluoro-glucosyl-enzyme [[intermediate]] and subsequent peptide mapping by LC/MS-MS <cite>miao1994</cite>. The [[catalytic nucleophile]] had been previously been mistakenly identified as Asp443 using a tritiated bromoconduritol epoxide <cite>dinur1986, legler1990</cite>, although subsequent kinetic analyses of site-directed mutants of Asp443 were not consistent with its role as the [[catalytic nucleophile]] <cite>grace1994</cite>. The [[general acid/base]] residue of human β-glucoerebrosidase is predicted to be Glu-274 <cite>durand1997</cite>. While this identification has not been experimentally verified through analysis of variant proteins created by mutation of that site, it is consistent with structural studies (below).

==Three-dimensional structures==
The three-dimensional structure of human β-glucocerebrosidase was first solved in 2003 <cite>dvir2003</cite>, and since then several different structures of this enzyme have been reported (reviewed in <cite>kacher2008</cite>). GH30 enzymes are members of the GHA clan fold, consistent with the classic (α/β)<sub>8</sub> TIM barrel fold with the two key active site glutamic acids located at the C-terminal ends of β-strands 4 (acid/base) and 7 (nucleophile) <cite>henrissat1995</cite>.

==Family Firsts==

;'''First [[catalytic nucleophile]] identification'''
:Human β-glucocerebrosidase by 2-fluoroglucose labelling <cite>#1</cite>
;'''First 3-D structure of a GH30 enzyme'''
:Human β-glucocerebrosidase <cite>#2</cite>

==References==
<biblio>
# grabowski2008 pmid=19094956
# grabowski1990 pmid=2127241
# oyama2002 pmid=12162562
# brunner2002 pmid=11909624
# miao1994 pmid=7908905
# dinur1986 pmid=3456607
# legler1990 pmid=2077872
# grace1994 pmid=8294487
# durand1997 pmid=9134434
# dvir2003 pmid=12792654
# kacher2008 pmid=18783340
# henrissat1995 pmid=7624375
</biblio>

[[Category:Glycoside Hydrolase Families|GH030]]

User:Franz St. John

2010-11-05T19:49:43Z

Franz St. John:

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria <cite>stjohn2006-1</cite>. Following an interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the X-ray Crystallography Core Facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of [[GH30]] and [[GH5]] enzymes <cite>stjohn2010</cite> and has determined the crystal structures of

* XynC, a [[GH30]] glucuronoxylan xylanohydrolase (previously of [[GH5]]) of ''Bacillus subtilis'' 168 <cite>stjohn2006-2, stjohn2009</cite>

* XynA<sub>1</sub>CD, the [[GH10]] catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 <cite>stjohn2006-1</cite>

----

<biblio>
# stjohn2006-1 pmid=16461704
# stjohn2010 pmid=20932833
# stjohn2006-2 pmid=17028274
# stjohn2009 pmid=19407387
</biblio>

[[Category:Contributors|St.John,Franz]]

User:Franz St. John

2010-11-04T10:11:07Z

Franz St. John:

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria <cite>REF1</cite>. Following an interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the X-ray Crystallography Core Facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of [[GH30]] and [[GH5]] enzymes <cite>REF2</cite> and has determined the crystal structures of

* XynC, a [[GH30]] glucuronoxylan xylanohydrolase (previously of [[GH5]]) of ''Bacillus subtilis'' 168 <cite>REF3, REF4</cite>

* XynA<sub>1</sub>CD, the [[GH10]] catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 <cite>REF1</cite>

----

<biblio>
# REF1 pmid=16461704
# REF2 pmid=20932833
# REF3 pmid=17028274
# REF4 pmid=19407387
</biblio>

[[Category:Contributors|St.John,Franz]]

User:Franz St. John

2010-10-26T20:38:04Z

Franz St. John:

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria <cite>REF1</cite>. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of [[GH30]] and [[GH5]] enzymes <cite>REF2</cite> and has determined the crystal structures of

* XynC, a [[GH30]] glucuronoxylan xylanohydrolase (previously of [[GH5]]) of ''Bacillus subtilis'' 168 <cite>REF3, REF4</cite>

* XynA<sub>1</sub>CD, the [[GH10]] catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 <cite>REF1</cite>

----

<biblio>

# REF1 PMID: 16461704
# REF2 PMID: 20932833
# REF3 PMID: 17028274
# REF4 PMID: 19407387

</biblio>

[[Category:Contributors|St.John,Franz]]

User:Franz St. John

2010-10-26T19:47:14Z

Franz St. John:

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria <cite>REF1</cite>. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of [[GH30]] and [[GH5]] enzymes <cite>REF4</cite> and has determined the crystal structures of

* XynC, a [[GH30]] glucuronoxylan xylanohydrolase (previously of [[GH5]]) of ''Bacillus subtilis'' 168 <cite>REF2, REF3</cite>

* XynA<sub>1</sub>CD, the [[GH10]] catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 <cite>REF1</cite>

----

<biblio>

# REF1 PMID: 16461704
# REF2 PMID: 17028274
# REF3 PMID: 19407387
# REF4 PMID: 20932833
</biblio>

[[Category:Contributors|St.John,Franz]]

User:Franz St. John

2010-10-19T18:17:48Z

Franz St. John:

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of GH30 and GH5 enzymes and has determined the crystal structures of

* XynC, a GH30 glucuronoxylan xylanohydrolase (previously of GH5) of ''Bacillus subtilis'' 168

* XynA<sub>1</sub>CD, the GH10 catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2

User:Franz St. John

2010-10-19T18:06:58Z

Franz St. John: Created page with "Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This res..."

Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional charaturization and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of GH30 and GH5 enzymes and has determined the crystal structures of

* XynC, a GH30 glucuronoxylan xylanohydrolase (previously of GH5) of ''Bacillus subtilis'' 168, in native and ligand bound forms

* XynA<sub>1</sub>CD, the GH10 catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2