期刊
PROTEIN SCIENCE
卷 25, 期 11, 页码 1942-1953出版社
WILEY
DOI: 10.1002/pro.3016
关键词
carboxylesterases; cholinesterases; cocaine esterases; cutinases; lysopholipases; phospholipases; triacylglycerol lipases
We classified the carboxylic ester hydrolases (CEHs) into families and clans by use of multiple sequence alignments, secondary structure analysis, and tertiary structure superpositions. Our work for the first time has fully established their systematic structural classification. Family members have similar primary, secondary, and tertiary structures, and their active sites and reaction mechanisms are conserved. Families may be gathered into clans by their having similar secondary and tertiary structures, even though primary structures of members of different families are not similar. CEHs were gathered from public databases by use of Basic Local Alignment Search Tool (BLAST) and divided into 91 families, with 36 families being grouped into five clans. Members of one clan have standard alpha/beta-hydrolase folds, while those of other two clans have similar folds but with different sequences of their beta-strands. The other two clans have members with six-bladed beta-propeller and three-alpha-helix bundle tertiary structures. Those families not in clans have a large variety of structures or have no members with known structures. At the time of writing, the 91 families contained 321,830 primary structures and 1378 tertiary structures. From these data, we constructed an accessible database: CASTLE (CArboxylic eSTer hydroLasEs, http://www.castle.cbe.iastate.edu).
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