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Carbohydrate Esterase Family 1
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- Author: ^^^Casper Wilkens^^^
- Responsible Curator:
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 central β-strands connected by α-helices [4].
Family Firsts
- First characterized
- Content is to be added here.
- 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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