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Glycoside Hydrolase Family 139
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| Glycoside Hydrolase Family GH139 | |
| Clan | none |
| Mechanism | unknown |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/GH139.html | |
Substrate specificities
Glycoside hydrolases of family 139 family display α-2-O-methyl-L-fucosidase activity. They are exclusively bacterial in origin. The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-acting 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 reported.
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 |