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Article

Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase.

Biochemistry - 2 Apr 2013

Xue Bo, Chow Jeng Yeong, Baldansuren Amgalanbaatar, Yap Lai Lai, Gan Yunn Hwen, Dikanov Sergei A, Robinson Robert C, Yew Wen Shan

Abstract excerpt

The in vitro evolution and engineering of quorum-quenching lactonases with enhanced reactivities was achieved using a thermostable GKL enzyme as a template, yielding the E101G/R230C GKL mutant with increased catalytic activity and a broadened substrate range [Chow, J. Y., Xue, B., Lee, K. H., Tung, A., Wu, L., Robinson, R. C., and Yew, W. S. (2010) J. Biol. Chem. 285, 40911-40920]. This enzyme possesses the...

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Identifiers

PMID: 23461395
DOI: 10.1021/bi4000904
PMCID: PMC3629905

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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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