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Difference between revisions of "Glycoside Hydrolase Family 139"

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* [[Author]]: ^^^Ana Luis^^^
 
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== Substrate specificities ==
 
== Substrate specificities ==
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-&alpha;-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II <cite>Ndeh2017</cite>.
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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-&alpha;-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 02:00, 14 February 2018

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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 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

  1. 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. 544, 65-70. DOI:10.1038/nature21725 | PubMed ID:28329766 | HubMed [Ndeh2017]