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Difference between revisions of "Glycoside Hydrolase Family 139"
| Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | Glycoside hydrolases of GH139 family ([http://www.cazy.org/GH139.html CAZy]) 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 | + | Glycoside hydrolases of the bacterial GH139 family ([http://www.cazy.org/GH139.html CAZy]) 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 == | ||
| − | The stereochemistry of the reaction catalyzed by | + | The stereochemistry of the reaction catalyzed by GH139 members has not yet been studied. |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 09:27, 13 February 2018
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.
- 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 (CAZy) 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 |