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Difference between revisions of "Glycoside Hydrolase Family 139"
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== Substrate specificities == | == Substrate specificities == | ||
| − | Glycoside hydrolases of the bacterial GH139 family | + | Glycoside hydrolases of the bacterial GH139 family display the novel α-2-O-methyl-L-fucosidase activity. The enzyme BT0984 from ''Bacteroides thetaiotaomicron'' is the only member of this family that has been characterized. This exo-enzyme targets the 2-O-methyl-L-fucose-α-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II <cite>Ndeh2017</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 01:00, 14 February 2018
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- Author: ^^^Ana Luis^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| Glycoside Hydrolase Family GH139 | |
| Clan | none |
| Mechanism | unknown |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH139.html | |
Substrate specificities
Glycoside hydrolases of the bacterial GH139 family display the novel α-2-O-methyl-L-fucosidase activity. The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-enzyme targets the 2-O-methyl-L-fucose-α-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II [1].
Kinetics and Mechanism
The stereochemistry of the reaction catalyzed by GH139 members has not yet been studied.
Catalytic Residues
Not known.
Three-dimensional structures
No three-dimensional structure has been solved for this family.
Family Firsts
- First stereochemistry determination
- Unknown.
- First catalytic nucleophile identification
- Unknown.
- First general acid/base residue identification
- Unknown.
- First 3-D structure
- Unknown.
References
- Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 |