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Article

Crystal structure and characterization of esterase Est25 mutants reveal improved enantioselectivity toward (S)-ketoprofen ethyl ester.

Applied microbiology and biotechnology - 1 Mar 2017

Kim Jinyeong, Seok Seung-Hyeon, Hong Eunsoo, Yoo Tae Hyeon, Seo Min-Duk, Ryu Yeonwoo

Abstract excerpt

Esterases comprise a group of enzymes that catalyze the cleavage and synthesis of ester bonds. They are important in biotechnological applications owing to their enantioselectivity, regioselectivity, broad substrate specificity, and the fact that they do not require cofactors. In a previous study, we isolated the esterase Est25 from a metagenomic library. Est25 showed catalytic activity toward the...

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PMID: 27915377
DOI: 10.1007/s00253-016-7989-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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