CAZypedia - User contributions [en-ca]

User:Jingjing Shen

2023-12-27T09:02:42Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite>, [[GH174]] <cite>Liu2023</cite> and [[GH187]] families <cite>Shen2024</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

Glycoside Hydrolase Family 187

2023-12-27T09:01:11Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''
|-
|'''Clan'''
|not known
|-
|'''Mechanism'''
|not known
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH187.html
|}
</div>


== Substrate specificities ==
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fuc''p''(2,4OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>) in an endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucans from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.
[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]

== Kinetics and Mechanism ==
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.

== Catalytic Residues ==
No catalytic residues have been identified in this glycoside hydrolase family at present.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2024 pmid=37940306
</biblio>


[[Category:Glycoside Hydrolase Families|GH187]]

Glycoside Hydrolase Family 187

2023-12-27T08:58:10Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''
|-
|'''Clan'''
|not known
|-
|'''Mechanism'''
|not known
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH187.html
|}
</div>


== Substrate specificities ==
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fuc''p''(2,4OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>) in an endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.
[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]

== Kinetics and Mechanism ==
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.

== Catalytic Residues ==
No catalytic residues have been identified in this glycoside hydrolase family at present.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2024 pmid=37940306
</biblio>


[[Category:Glycoside Hydrolase Families|GH187]]

Glycoside Hydrolase Family 187

2023-12-27T08:56:21Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''
|-
|'''Clan'''
|not known
|-
|'''Mechanism'''
|not known
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH187.html
|}
</div>


== Substrate specificities ==
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fucp(2,4OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fucp-1→3-α-L-Fucp(2OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fucp(2OSO<sub>3</sub><sup>-</sup>) in an endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.
[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]

== Kinetics and Mechanism ==
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.

== Catalytic Residues ==
No catalytic residues have been identified in this glycoside hydrolase family at present.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2024 pmid=37940306
</biblio>


[[Category:Glycoside Hydrolase Families|GH187]]

Glycoside Hydrolase Family 187

2023-12-27T08:42:57Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''
|-
|'''Clan'''
|not known
|-
|'''Mechanism'''
|not known
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH187.html
|}
</div>


== Substrate specificities ==
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fucp(2,4OSO3-)-1→3-α-L-Fucp-1→3-α-L-Fucp(2OSO3-)-1→3-α-L-Fucp(2OSO<sub>3</sub><sup>-</sup>) in a endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.
[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]

== Kinetics and Mechanism ==
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.

== Catalytic Residues ==
No catalytic residues have been identified in this glycoside hydrolase family at present.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2024 pmid=37940306
</biblio>


[[Category:Glycoside Hydrolase Families|GH187]]

File:Figure 1.jpg

2023-12-27T08:31:58Z

Jingjing Shen: Figure 1. The phylogenetic tree of GH187 homologues. Sequences comfirmed to exhibit α-1,3-L-fucanase activity were higilighted in red triangles.

== Summary ==
Figure 1. The phylogenetic tree of GH187 homologues. Sequences comfirmed to exhibit α-1,3-L-fucanase activity were higilighted in red triangles.

User:Jingjing Shen

2023-12-27T08:28:57Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite>,[[GH174]] <cite>Liu2023</cite> and [[GH187]] families <cite>Shen2024</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-12-27T08:27:34Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite>,[[GH174]] families <cite>Liu2023</cite> and [[GH187]] families <cite>Shen2024</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-12-27T08:23:23Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite>,[[GH174]] families <cite>Liu2023</cite> and [[GH187]] families <cite>Shen 2024</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-12-27T08:19:28Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite>,[[GH174]] families <cite>Liu2023</cite> and [[GH187]] families <cite>Shen 2024</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-12-27T08:17:06Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite> and [[GH174]] families <cite>Liu2023</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2024 pmid=37940306
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

Glycoside Hydrolase Family 187

2023-12-27T08:09:01Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH187.html
|}
</div>


== Substrate specificities ==
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fucp(2,4OSO3-)-1→3-α-L-Fucp-1→3-α-L-Fucp(2OSO3-)-1→3-α-L-Fucp(2OSO<sub>3</sub><sup>-</sup>) in a random endo-acting manner. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from Holothuria tubulosa and Isostichopus badionotus, namely WP_159020740.1.

Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''

In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.

== Kinetics and Mechanism ==
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol.

== Catalytic Residues ==
No catalytic residues have been identified in this glycoside hydrolase family at present.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].
</biblio>


[[Category:Glycoside Hydrolase Families|GH187]]

User:Jingjing Shen

2023-06-18T17:18:15Z

Jingjing Shen:

[[Image:Shen.jpg|200px|right]]
Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of glycoside hydrolases. She discovered and characterized the first member of [[GH168]] <cite>Shen2020</cite> and [[GH174]] families <cite>Liu2023</cite>, and contributed to the studies related to members of the following families:
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite>
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582
#Shen2018 pmid=29355636
#Shen2017 pmid=28760444
</biblio>


[[Category:Contributors|Shen,Jingjing]]

Glycoside Hydrolase Family 168

2023-06-18T14:05:41Z

Jingjing Shen:

{{CuratorApproved}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1 <cite>Shen2020</cite>.
[[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis <cite>Shen2020</cite>.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A <cite>Shen2020</cite>.
[[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences were indicated with black triangles.]]

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

Glycoside Hydrolase Family 168

2023-06-18T14:02:45Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1 <cite>Shen2020</cite>.
[[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis <cite>Shen2020</cite>.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A <cite>Shen2020</cite>.
[[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences were indicated with black triangles.]]

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

Glycoside Hydrolase Family 168

2023-06-18T14:02:09Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner <cite>Shen2020</cite>. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.
[[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis <cite>Shen2020</cite>.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A <cite>Shen2020</cite>.
[[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences were indicated with black triangles.]]

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

Glycoside Hydrolase Family 168

2023-06-18T13:59:26Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner <cite>Shen2020</cite>. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.
[[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A.
[[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences were indicated with black triangles.]]

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

Glycoside Hydrolase Family 168

2023-06-18T13:57:48Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a random endo-acting manner <cite>Shen2020</cite>. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.
[[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A.
[[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences were indicated with black triangles.]]

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

File:Catalytic residues.png

2023-06-18T13:51:08Z

Jingjing Shen:

File:Tree of GH168.png

2023-06-18T13:50:50Z

Jingjing Shen:

Glycoside Hydrolase Family 168

2023-06-18T13:49:39Z

Jingjing Shen:

{{UnderConstruction}}
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]

----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH168'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH168.html
|}
</div>


== Substrate specificities ==
Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium Wenyingzhuangia funcanilytica CZ1127T, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a random endo-acting manner <cite>Shen2020</cite>. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from Isostichopus badionotus, namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.

== Kinetics and Mechanism ==
As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis.

== Catalytic Residues ==
Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A.

== Three-dimensional structures ==
No three-dimensional structure has been solved in this glycoside hydrolase family at present.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Not yet identified.

== References ==
<biblio>
#Shen2020 pmid=32849348
</biblio>


[[Category:Glycoside Hydrolase Families|GH168]]

User:Jingjing Shen

2023-06-18T13:27:56Z

Jingjing Shen:

File:Shen.jpg

2023-06-18T13:25:22Z

Jingjing Shen:

User:Jingjing Shen

2023-06-18T13:23:03Z

Jingjing Shen:

Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of of glycoside hydrolase. She discovered and characterized the first member of GH168 <cite>Shen2020</cite> and GH174 families <cite>Liu2023</cite>.

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582

</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-06-18T13:21:58Z

Jingjing Shen:

Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of functional domains of glycoside hydrolase. She discovered and characterized the first member of GH168 <cite>Shen2020</cite> and GH174 families <cite>Liu2023</cite>.

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582

</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-06-18T13:20:02Z

Jingjing Shen:

Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of functional domains of glycoside hydrolase. She discovered and characterized the first member of GH168 [1] and GH174 families [2].

----

<biblio>
#Shen2020 pmid=32849348
#Liu2023 pmid=36746582

</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-06-18T13:19:10Z

Jingjing Shen:

Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of functional domains of glycoside hydrolase. She discovered and characterized the first member of GH168 [1] and GH174 families [2].

----

<biblio>
#Shen2020 pmid=32849348

</biblio>


[[Category:Contributors|Shen,Jingjing]]

User:Jingjing Shen

2023-06-18T13:16:37Z

Jingjing Shen:

Jingjing Shen is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. Her research focuses on the gene-mining and characterization of functional domains of glycoside hydrolase. She discovered and characterized the first member of GH168 [1] and GH174 families [2].

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Shen,Jingjing]]