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Difference between revisions of "Glycoside Hydrolase Family 187"
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== 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 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...)'' | 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...)'' | ||
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== 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. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | No catalytic residues have been identified in this glycoside hydrolase family at present. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | No three-dimensional structure has been solved in this glycoside hydrolase family at present. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not yet identified. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: Not yet identified. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Not yet identified. |
| − | ;First 3-D structure: | + | ;First 3-D structure: Not yet identified. |
== References == | == References == | ||
Revision as of 01:09, 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 | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| http://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 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: [1, 2].
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
-
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. DOI:10.1042/BIO03004026.
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |