CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 6

2010-03-05T16:35:15Z

Kathleen Piens:

{{UnderConstruction}}
* [[Author]]: ^^^Kathleen Piens^^^ and ^^^Gideon Davies^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH6'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|acid known, base debated
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH6.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolase (EC [{{EClink}}3.2.1.91 3.2.1.91]) activity has been reported for both bacterial and eukaryotic members of this family.

== Kinetics and Mechanism ==
Family 6 enzymes are [[inverting]] enzymes, as first shown by NMR <cite>Knowles1988</cite> on Cellobiohydrolase II (CBH II; Cel6A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' <cite>Kuhls1996</cite>).

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

----
{| {{Prettytable}} style="text-align:left"
|+ Table. Putative catalytic residues of some representatives in GH family 6<br>(with biochemical characterization of wt and mutant enzymes).
! Proposed role
! ''Cf''Cel6A (endo)
! ''Hi''Cel6A (exo)
! ''Hj''Cel6A (exo)
! ''Tf''Cel6A (endo)
! ''Tf''Cel6B (exo)
|-
| Substrate distortion
| Tyr210
| Tyr174
| Tyr169
| Tyr73
| Tyr220
|-
| Increase in pKa acid/Catalytic base
| Asp216
| Asp180
| Asp175
| Asp79
| Asp226
|-
| Proton network
| Gly222?
| Ser186
| Ser181
| Ser85
| Ser232
|-
| Catalytic acid
| Asp252
| Asp226
| Asp221
| Asp117
| Asp274
|-
| Catalytic base/substrate binding
| Asp392
| Asp405
| Asp401
| Asp265
| Asp497
|}
----

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel6A by NMR <cite>Knowles1988</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation.
;First 3-D structure: The catalytic core domain of the ''Trichoderma reesei'' (the organism now known as ''Hypocrea jecorina'') cellobiohydrolase II by the Jones group <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite>

== References ==
<biblio>
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]
#Kuhls1996 pmid=8755548
#Rouvinen1990 pmid=2377893
#Spezio1993 pmid=8399160

</biblio>

[[Category:Glycoside Hydrolase Families|GH006]]

Glycoside Hydrolase Family 6

2010-03-05T15:47:49Z

Kathleen Piens:

{{UnderConstruction}}
* [[Author]]: ^^^Kathleen Piens^^^ and ^^^Gideon Davies^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH6'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|acid known, base debated
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH6.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolase (EC [{{EClink}}3.2.1.91 3.2.1.91]) activity has been reported for both bacterial and eukaryotic members of this family.

== Kinetics and Mechanism ==
Family 6 enzymes are [[inverting]] enzymes, as first shown by NMR <cite>Knowles1988</cite> on Cellobiohydrolase II (CBH II; Cel6A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' <cite>Kuhls1996</cite>).

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

----
{| {{Prettytable}} style="text-align:left"
|+ Table. Putative catalytic residues of some representatives in GH family 6<br>(with biochemical characterization of wt and mutant enzymes).
! Proposed role
! ''Cf''Cel6A (endo)
! ''Hi''Cel6A (exo)
! ''Hj''Cel6A (exo)
! ''Tf''Cel6A (endo)
! ''Tf''Cel6B (exo)
|-
| Substrate distortion
| Tyr210
| Tyr174
| Tyr169
| Tyr73
| Tyr220
|-
| Increase in pKa acid/Catalytic base
| Asp216
| Asp180
| Asp175
| Asp79
| Asp226
|-
| Proton network
| Gly222?
| Ser186
| Ser181
| Ser85
| Ser232
|-
| Catalytic acid
| Asp252
| Asp226
| Asp221
| Asp117
| Asp274
|-
| Catalytic base/substrate binding
| Asp392
| Asp405
| Asp401
| Asp265
| Asp497
|}
----

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 senetence) explanation.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation.
;First 3-D structure: The catalytic core domain of the ''Trichoderma reesei'' (the organism now known as ''Hypocrea jecorina'') cellobiohydrolase II by the Jones group <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite>

== References ==
<biblio>
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]
#Kuhls1996 pmid=8755548
#Rouvinen1990 pmid=2377893
#Spezio1993 pmid=8399160

</biblio>

[[Category:Glycoside Hydrolase Families|GH006]]

Glycoside Hydrolase Family 6

2010-03-05T15:21:32Z

Kathleen Piens:

{{UnderConstruction}}
* [[Author]]: ^^^Kathleen Piens^^^ and ^^^Gideon Davies^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH6'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|acid known, base debated
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH6.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolase (EC [{{EClink}}3.2.1.91 3.2.1.91]) activity has been reported for both bacterial and eukaryotic members of this family.

== Kinetics and Mechanism ==
Family 6 enzymes are [[inverting]] enzymes, as first shown by NMR <cite>Knowles1988</cite> on Cellobiohydrolase II (CBH II; Cel6A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' <cite>Kuhls1996</cite>).

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

----
{| {{Prettytable}} style="text-align:left"
|+ Table. Putative catalytic residues of some representatives in GH family 6<br>(with biochemical characterization of wt and mutant enzymes).
! Proposed role
! ''Cf''Cel6A (endo)
! ''Hi''Cel6A (exo)
! ''Hj''Cel6A (exo)
! ''Tf''Cel6A (endo)
! ''Tf''Cel6B (exo)
|-
| Substrate distortion
| Asp210
| Tyr174
| Tyr169
| Tyr73
| Tyr220
|-
| Increase in pKa acid/Catalytic base
| Asp216
| Asp180
| Asp175
| Asp79
| Asp226
|-
| Proton network
| Gly222
| Ser186
| Ser181
| Ser85
| Asp232
|-
| Catalytic acid
| Asp252
| Asp226
| Asp221
| Asp117
| Asp274
|-
| Catalytic base/substrate binding
| Asp392
| Asp405
| Asp401
| Asp265
| Asp497
|}
----

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 senetence) explanation.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation.
;First 3-D structure: The catalytic core domain of the ''Trichoderma reesei'' (the organism now known as ''Hypocrea jecorina'') cellobiohydrolase II by the Jones group <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite>

== References ==
<biblio>
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]
#Kuhls1996 pmid=8755548
#Rouvinen1990 pmid=2377893
#Spezio1993 pmid=8399160

</biblio>

[[Category:Glycoside Hydrolase Families|GH006]]

Glycoside Hydrolase Family 6

2010-03-05T15:13:54Z

Kathleen Piens:

{{UnderConstruction}}
* [[Author]]: ^^^Kathleen Piens^^^ and ^^^Gideon Davies^^^
* [[Responsible Curator]]: ^^^Gideon Davies^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH6'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|acid known, base debated
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH6.html
|}
</div>


== Substrate specificities ==
[[glycoside hydrolases]] of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolase (EC [{{EClink}}3.2.1.91 3.2.1.91]) activity has been reported for both bacterial and eukaryotic members of this family.

== Kinetics and Mechanism ==
Family 6 enzymes are [[inverting]] enzymes, as first shown by NMR <cite>Knowles1988</cite> on Cellobiohydrolase II (CBH II; Cel6A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' <cite>Kuhls1996</cite>).

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

----
{| {{Prettytable}} style="text-align:left"
|+ Table. Putative catalytic residues of some representatives in GH family 6<br>(with biochemical characterization of wt and mutant enzymes).
! Proposed role
! ''Cf''Cel6A (endo)
! ''Hi''Cel6A (exo)
! ''Hj''Cel6A (exo)
! ''Tf''Cel6A (endo)
! ''Tf''Cel6B (exo)
|-
| Substrate distortion
| Asp210
| Tyr174
| Tyr169
| Tyr73
| Tyr220
|-
| Increase in pKa acid/Catalytic base
| Asp216
| Asp180
| Asp175
| Asp79
| Asp226
|-
| Proton network
| Gly222
| Ser186
| Ser181
| Ser85
| Asp232
|-
| Catalytic acid
| Asp252
| Asp226
| Asp221
| Asp117
| Asp274
|-
| Catalytic base/substrate binding
| Asp392
| Asp405
| Asp401
| Asp265
| Asp497
|}
----

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>1</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation <cite>2</cite>.
;First 3-D structure: The catalytic core domain of the ''Trichoderma reesei'' (the organism now known as ''Hypocrea jecorina'') cellobiohydrolase II by the Jones group <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite>

== References ==
<biblio>
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]
#Kuhls1996 pmid=8755548
#Rouvinen1990 pmid=2377893
#Spezio1993 pmid=8399160
#3 isbn=978-0-240-52118-3
#4 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]

</biblio>

[[Category:Glycoside Hydrolase Families|GH006]]

User:Kathleen Piens

2009-11-11T21:29:09Z

Kathleen Piens:

[[File:Kathleen08.JPG|200px|thumb|left]] I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close collaboration with Dr. ^^^Harry Brumer^^^ (KTH), was focusing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. [[User:Jerry Stahlberg|Jerry Ståhlberg]] and Dr. ^^^Mats Sandgren^^^.

[[Category:Contributors|Piens, Kathleen]]

User:Kathleen Piens

2009-11-11T21:10:45Z

Kathleen Piens:

[[File:Kathleen08.jpg|left]] I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close collaboration with Dr. ^^^Harry Brumer^^^ (KTH), was focusing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. [[User:Jerry Stahlberg|Jerry Ståhlberg]] and Dr. ^^^Mats Sandgren^^^.

[[Category:Contributors|Piens, Kathleen]]

File:Kathleen08.JPG

2009-11-11T21:08:51Z

Kathleen Piens:

File:Lauterbach1 032.JPG

2009-11-11T21:05:25Z

Kathleen Piens: uploaded a new version of "File:Lauterbach1 032.JPG"

User:Kathleen Piens

2009-11-11T21:02:26Z

Kathleen Piens:

[[File:Lauterbach1 032.jpg|left]] I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close collaboration with Dr. ^^^Harry Brumer^^^ (KTH), was focusing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. [[User:Jerry Stahlberg|Jerry Ståhlberg]] and Dr. ^^^Mats Sandgren^^^.

[[Category:Contributors|Piens, Kathleen]]

User:Kathleen Piens

2009-11-11T20:59:38Z

Kathleen Piens:

[[File:Lauterbach1_32.jpg|left]] I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close collaboration with Dr. ^^^Harry Brumer^^^ (KTH), was focusing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. [[User:Jerry Stahlberg|Jerry Ståhlberg]] and Dr. ^^^Mats Sandgren^^^.

[[Category:Contributors|Piens, Kathleen]]

File:Lauterbach1 032.JPG

2009-11-11T20:31:31Z

Kathleen Piens:

User:Kathleen Piens

2009-10-15T09:00:04Z

Kathleen Piens:

I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close collaboration with Dr. Harry Brumer (KTH), was focusing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. Jerry Ståhlberg and Dr. Mats Sandgren.

User:Kathleen Piens

2009-10-15T08:59:28Z

Kathleen Piens:

User:Kathleen Piens

2009-10-15T08:57:59Z

Kathleen Piens:

User:Kathleen Piens

2009-10-15T08:56:34Z

Kathleen Piens:

I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay in the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close colaboration with Dr. Harry Brumer (KTH), was focussing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden in the group of Prof. Jerry Ståhlberg and Dr. Mats Sandgren.

User:Kathleen Piens

2009-10-15T08:53:44Z

Kathleen Piens:

I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me in 2002 to Stockholm, Sweden for a 3-year postdoctoral stay at the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close colaboration with Dr. Harry Brumer (KTH) was focussing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences in Uppsala, Sweden in the group of Prof Jerry Ståhlberg and Dr. Mats Sandgren.

User:Kathleen Piens

2009-10-15T08:53:00Z

Kathleen Piens: Created page with 'I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I comp…'

I obtained a Master of Science degree in Organic Chemistry at Ghent University (UGent), Belgium in 1991. I joined the group of Prof. Marc Claeyssens in 1995 at UGent where I completed my Ph.D. in 2001 on "Cellulolytic enzymes and specific ligands: a structure-function analysis". An EU Marie Curie Fellowship brought me to Stockholm, Sweden for a 3-year postdoctoral stay at the group of Prof. Tuula Teeri, Department of Wood Biotechnology (currently School of Biotechnology), Royal Institute of Technology (KTH). My project, in close colaboration with Dr. Harry Brumer (KTH) was focussing on the determinants of transglycosylating versus hydrolytic activity in xyloglucan endotransglycosylases. In 2005 I moved back to Belgium to accept a Doctor Assistant position at the Department of Biochemistry and Microbiology, UGent, to lead the glycobiology research group of Prof. Em. Marc Claeyssens, who retired in Oct 2005. Presently I am continuing my research on the characterization of carbohydrate-active enzymes and the development of kinetic assays at the Swedish University of Agricultural Sciences in Uppsala, Sweden in the group of Prof Jerry Ståhlberg and Dr. Mats Sandgren.