Carbohydrate Esterase Family 1

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• Author: ^^^Casper Wilkens^^^
• Responsible Curator:

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Carbohydrate Esterase Family 1
Clan	GH-x
Mechanism	retaining/inverting
Active site residues	known/not known
CAZy DB link
https://www.cazy.org/CE1.html

Substrate specificities

Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol O-acyltransferases (EC 2.3.1.20), and thehalose 6-O-mycolyltransferases (EC 2.3.1.122) and others [1].

Kinetics and Mechanism

Content is to be added here. Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate [2] Ferulic acid esterases hydrolyze the ester bond linking the ferulic acid to the arabinose moiety, which decorate certain types of xylan.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

CE1's are members of the α/β-hydrolase superfamily [3], which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices [4]. The crystal structure of 9 CE1s have been determined - 4 mycosyltransferases, 4 ferulic acid esterases and 1 acetyl xylan esterase [1].

Family Firsts

First characterized

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First mechanistic insight

The crystal structure of Mycobacterium tuberculosis H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad [3].

First 3-D structure

Mycobacterium tuberculosis H37Rv mycolyltransferase crystal structure in 2000 [3].

References

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