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Article

Enhanced enzyme thermostability of a family I.3 lipase LipSR1 by T118A mutation at the calcium-binding site.

Biotechnology letters - 1 Sept 2023

Jiang Shijie, Zhou Zhengfu, Han Jiahui, Fan Qingfeng, Long Zhijian, Wang Jin

Abstract excerpt

OBJECTIVES: The lipase gene lipSR1 isolated from oil-contaminated soil exhibits high hydrolytic activity for short-chain fatty acid substrates. A single calcium ion is required to anchor the lid of LipSR1 in an open conformation by coordination with two aspartate residues and three other residues in the lid. The lid of LipSR1 is anchored by Ca2+, which is coordinated by side-chain carboxyl oxygens of Asp153 and...

Topics

Lipase
Calcium
Binding Sites
Mutagenesis, Site-Directed
Mutation
Enzyme Stability

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 37439931
DOI: 10.1007/s10529-023-03413-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-37439931-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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