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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.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
CE1's are members of the α/β-hydrolase superfamily [2], which are comprised of central β-strands connected by α-helices [3].
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 [2].
- First 3-D structure
- Mycobacterium tuberculosis H37Rv mycolyltransferase crystal structure in 2000 [2].
References
- Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, and Henrissat B. (2014). The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42(Database issue):D490-5. DOI:10.1093/nar/gkt1178 |
- Ronning DR, Klabunde T, Besra GS, Vissa VD, Belisle JT, and Sacchettini JC. (2000). Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nat Struct Biol. 2000;7(2):141-6. DOI:10.1038/72413 |
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pmid1409539