CAZypedia - User contributions [en-ca]

Carbohydrate Esterase Family 15

2019-01-28T13:39:36Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Spanikova2006 pmid=16876163
#Arnlingbaath2018 pmid=30083226
#Desanti2016 pmid=27433797
#Mosbech2018 pmid=29560026
#Derrico2016 pmid=26712478
#Arnlingbaath2016 pmid=27397104
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
#Desanti2017 pmid=29222424
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:36:56Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Spanikova2006 pmid=16876163
#Arnlingbaath2018 pmid=30083226
#Desanti2016 pmid=27433797
#Mosbech2018 pmid=29560026
#Derrico2016 pmid=26712478
#Arnlingbaath2016 pmid=27397104
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:33:53Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Spanikova2006 pmid=16876163
#Arnlingbaath2018 pmid=30083226
#Desanti2016 pmid=27433797
#Mosbech2018 pmid=29560026
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:30:21Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018 </cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:27:31Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018 </cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser (Pokkuluri 2011, Charavgi 2013, de Santi 2017, Arnling Bååth 2018). The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold (de Santi 2017). A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis (Arnling Bååth 2018).

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:22:26Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018 </cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: TrGE (Cip2) from T. reesei(Hypocrea jecorina) (PDB: 3pic) (Pokkuluri et al., 2011), StGE2 from Thermothelomyces thermophila(previously Sporotrichum thermophile) (PDB: 4g4g, 4g4i and 4g4j) (Charavgi et al., 2013), MZ0003 (PDB: 6ehn; cloned from a marine metagenome) (De Santi et al., 2017), OtCE15A (PDB: 6grw and 6gs0) and SuCE15C (PDB: 6gry and 6gu8) (Arnling Bååth 2018). All structurally determined CE15 enzymes share an a/bhydrolase fold, consisting of a three-layer a-b-asandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures (de Santi 2017, Arnling Bååth 2018).

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser (Pokkuluri 2011, Charavgi 2013, de Santi 2017, Arnling Bååth 2018). The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold (de Santi 2017). A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis (Arnling Bååth 2018).

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:17:28Z

Jenny Arnling Bååth:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ScGE1 from the white-rot fungus Schizophyllum commune, and the activity was demonstrated by TLC on a methyl ester of 4-O-methyl-D-glucuronic acid (Spanikova 2006). While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate (Arnling Bååth 2018). Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities (de Santi 2016, Mosbech 2018). The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass (D’Errico 2016, Arnling Bååth 2016, Mosbech 2018).

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: TrGE (Cip2) from T. reesei(Hypocrea jecorina) (PDB: 3pic) (Pokkuluri et al., 2011), StGE2 from Thermothelomyces thermophila(previously Sporotrichum thermophile) (PDB: 4g4g, 4g4i and 4g4j) (Charavgi et al., 2013), MZ0003 (PDB: 6ehn; cloned from a marine metagenome) (De Santi et al., 2017), OtCE15A (PDB: 6grw and 6gs0) and SuCE15C (PDB: 6gry and 6gu8) (Arnling Bååth 2018). All structurally determined CE15 enzymes share an a/bhydrolase fold, consisting of a three-layer a-b-asandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures (de Santi 2017, Arnling Bååth 2018).

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser (Pokkuluri 2011, Charavgi 2013, de Santi 2017, Arnling Bååth 2018). The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold (de Santi 2017). A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis (Arnling Bååth 2018).

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

Carbohydrate Esterase Family 15

2019-01-28T13:15:28Z

Jenny Arnling Bååth:

Carbohydrate Esterase Family 15

2019-01-28T13:11:08Z

Jenny Arnling Bååth:

User:Jenny Arnling Bååth

2018-11-17T14:04:06Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a MSc in Biotechnology from Lund University, which involved a year at Vienna University of Technology and work on the lactose metabolism in ''T. reesei'' <cite>Ivanova2013</cite>. In 2014, I started my PhD studies at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. ^^^Johan Larsbrink^^^. I am currently finalising my PhD thesis and will graduate in February 2019. My research concerns the controlled deconstruction of plant biomass <cite>ArnlingBaath2018b</cite>, in particular glucuronoyl esterases <cite>ArnlingBaath2016, ArnlingBaath2018a</cite> belonging to [[Carbohydrate Esterase Family 15]].

I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-11-17T14:03:15Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a MSc in Biotechnology from Lund University, which involved a year at Vienna University of Technology and work on the lactose metabolism in ''T. reesei'' <cite>Ivanova2013</cite>. In 2014, I started as a PhD student at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. ^^^Johan Larsbrink^^^. I am currently finalising my PhD thesis and will graduate in February 2019. My research concerns the controlled deconstruction of plant biomass <cite>ArnlingBaath2018b</cite>, in particular glucuronoyl esterases <cite>ArnlingBaath2016, ArnlingBaath2018a</cite> belonging to [[Carbohydrate Esterase Family 15]].

I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-11-17T13:49:26Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a master's degree in Biotechnology from Lund University, Sweden. In 2014, I started as a PhD student at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. ^^^Johan Larsbrink^^^. I am currently finalising my PhD thesis and will graduate in February 2019. My research concerns the controlled deconstruction of plant biomass <cite>ArnlingBaath2018b</cite>, in particular glucuronoyl esterases <cite>ArnlingBaath2016, ArnlingBaath2018a</cite> belonging to [[Carbohydrate Esterase Family 15]].

I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-11-17T11:39:19Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a master's degree in biotechnology from Lund University, Sweden. In 2014, I started as a PhD student at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. ^^^Johan Larsbrink^^^. I am currently finalising my PhD thesis and will graduate in February 2019. My research mainly concerns characterisation of glucuronoyl esterases, belonging to [[Carbohydrate Esterase Family 15]].

I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-11-17T11:35:12Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a master's degree in biotechnology from Lund University, Sweden. In 2014, I started as a PhD student at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. ^^^Johan Larsbrink^^^. My research mainly concerns glucuronoyl esterases, belonging to [[Carbohydrate Esterase Family 15]]. I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-11-17T11:31:05Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
I hold a master's degree in biotechnology from Lund University, Sweden. Currently, I am a PhD student at the division of Industrial biotechnology at Chalmers Technical University, Gothenburg, Sweden. My research mainly concerns glucuronoyl esterases, belonging to [[Carbohydrate Esterase Family 15]]. I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.

== Selected papers ==

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-10-28T13:09:39Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

I hold a master's degree in biotechnology from Lund University, Sweden. Currently, I am a PhD student at the division of Industrial biotechnology at Chalmers Technical University, Gothenburg, Sweden. My research mainly concerns glucuronoyl esterases, belonging to the carbohydrate esterase family 15. I have been involved in structure-function studies of bacterial CE15 enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of CE15 enzymes on model substrates and native lignin-carbohydrate ester bonds.

----

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#Lee2018 pmid=29110486
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-10-28T13:06:19Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

I hold a master's degree in biotechnology from Lund University, Sweden. Currently, I am a PhD student at the division of Industrial biotechnology at Chalmers Technical University, Gothenburg, Sweden. My research mainly concerns glucuronoyl esterases, belonging to the carbohydrate esterase family 15. I have been involved in structure-function studies of bacterial CE15 enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of CE15 enzymes on model substrates and native lignin-carbohydrate ester bonds.

----

<biblio>
#ArnlingBaath2018a pmid=30083226
#ArnlingBaath2018b pmid=29713374
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-10-28T13:05:20Z

Jenny Arnling Bååth:

User:Jenny Arnling Bååth

2018-10-28T12:33:01Z

Jenny Arnling Bååth:

User:Jenny Arnling Bååth

2018-10-28T12:31:55Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

I hold a master's degree in biotechnology from Lund University, Sweden. Currently, I am a PhD student in the division of Industrial biotechnology at Chalmers Technical University, Gothenburg, Sweden. My research mainly concerns glucuronoyl esterases, belonging to the carbohydrate esterase family 15. I have been involved in structure-function studies of bacterial CE15 enzymes <cite>ArnlingBaath2018</cite>, where my main contribution has been biochemical characterisation of CE15 enzymes on model substrates and native lignin-carbohydrate ester bonds.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#ArnlingBaath2018 pmid=30083226
#ArnlingBaath2018 pmid=29713374
#ArnlingBaath2016 pmid=27397104
#Ivanova2013 pmid=23690947

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-10-28T12:26:28Z

Jenny Arnling Bååth:

[[Image:Jenny arnling bååth.jpg|200px|right]]

I hold a master's degree in biotechnology from Lund University, Sweden. Currently, I am a PhD student in the division of Industrial biotechnology at Chalmers Technical University, Gothenburg, Sweden. My research mainly concerns glucuronoyl esterases, belonging to the carbohydrate esterase family 15. I have been involved in structure-function studies of bacterial CE15 enzymes <cite>ArnlingBaath2018</cite>, where my main contribution has been biochemical characterisation of CE15 enzymes on model substrates and native lignin-carbohydrate ester bonds.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#ArnlingBaath2018 pmid=30083226

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

User:Jenny Arnling Bååth

2018-10-23T20:38:10Z

Jenny Arnling Bååth:

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

Jenny Arnling Bååth holds a master's degree in biotechnology from Lund University. She is currently a PhD student at the division of industrial biotechnology at Chalmers University of Technology.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Arnling-Bååth2018 pmid=30083226

</biblio>


[[Category:Contributors|Arnling-Bååth,Jenny]]

File:Jenny arnling bååth.jpg

2018-10-23T20:22:21Z

Jenny Arnling Bååth: