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Difference between revisions of "Glycoside Hydrolase Family 168"
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* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]] | * [[Author]]: [[User:Jingjing Shen|Jingjing Shen]] | ||
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]] | * [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]] | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | Members of | + | Members of GH168 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 hydrolyzes 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, [http://www.cazy.org/GH168_characterized.html five homologues of Fun168A display activities toward sulfated fucan] from ''Isostichopus badionotus'' <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.]] | [[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 == | == Kinetics and Mechanism == | ||
| − | + | ''W. funcanilytica'' Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. This transglycosylating activity implied a [[retaining]] mechanism of catalysis <cite>Shen2020</cite>. | |
== Catalytic Residues == | == 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 | + | Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants of ''W. funcanilytica'' Fun168A, D206E and E264Q, were inactive on Ib-FUC, indicating that D206 and E264 were critical for activity <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 | + | [[File:catalytic residues.png|thumb|'''Figure 2. Multiple sequence alignments of residues in GH168 homologues.''' The strictly conserved residues in all sequences are indicated with black triangles.]] |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | No three-dimensional structure has been solved in this | + | No three-dimensional structure has been solved in this family at present. |
== Family Firsts == | == Family Firsts == | ||
Latest revision as of 11:23, 18 June 2023
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
| Glycoside Hydrolase Family GH168 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH168.html | |
Substrate specificities
Members of GH168 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 hydrolyzes 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 [1].
Kinetics and Mechanism
W. funcanilytica Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. This transglycosylating activity implied a retaining mechanism of catalysis [1].
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 of W. funcanilytica Fun168A, D206E and E264Q, were inactive on Ib-FUC, indicating that D206 and E264 were critical for activity [1].
Three-dimensional structures
No three-dimensional structure has been solved in this 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.