Alpha/beta‐hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families
@article{Dimitriou2017AlphabetahydrolasesAU, title={Alpha/beta‐hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families}, author={Polytimi S Dimitriou and Alexander I. Denesyuk and Seiji Takahashi and Satoshi Yamashita and Mark S. Johnson and Toru Nakayama and Konstantin A. Denessiouk}, journal={Proteins: Structure}, year={2017}, volume={85}, pages={1845 - 1855} }
The alpha/beta‐hydrolases are a family of acid‐base‐nucleophile catalytic triad enzymes with a common fold, but using a wide variety of substrates, having different pH optima, catalyzing unique catalytic reactions and often showing improved chemical and thermo stability. The ABH enzymes are prime targets for protein engineering. Here, we have classified active sites from 51 representative members of 40 structural ABH fold families into eight distinct conserved geometries. We demonstrate the…
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