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Difference between revisions of "Glycoside Hydrolase Family 187"
| Line 13: | Line 13: | ||
|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | | | + | |not known |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |not known |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |not known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 30: | Line 30: | ||
== Substrate specificities == | == 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 | + | 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 == | == 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. | + | 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 == | == Catalytic Residues == | ||
| Line 53: | Line 50: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Shen2024 pmid=37940306 |
| − | |||
</biblio> | </biblio> | ||
<!-- Do not delete this Category tag --> | <!-- Do not delete this Category tag --> | ||
[[Category:Glycoside Hydrolase Families|GH187]] | [[Category:Glycoside Hydrolase Families|GH187]] | ||
Revision as of 00:42, 27 December 2023
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
| Glycoside Hydrolase Family GH187 | |
| Clan | not known |
| Mechanism | not known |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH187.html | |
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(2OSO3-) in a endo-acting manner [1]. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from Holothuria tubulosa and Isostichopus badionotus, namely WP_159020740.1 [1].
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 [1].
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.