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Article

Studying the active site pocket of Staphylococcus hyicus lipase by site-directed mutagenesis.

Biochemical and biophysical research communications - 4 Dec 1996

Chang R C, Chen J C, Shaw J F

Abstract excerpt

Site-directed mutagenesis of a previously constructed, recombinant Staphylococcus hyicus lipase (49 kDa) showed that Val363 played a role in catalysis and substrate-binding. In comparison with wild type enzyme, the 64% and 89% decrease in the catalytic efficiency (kcat/Km) of the V363N and V363A enzymes, respectively, were largely caused by a 3.5- and 5.5-fold increase in the substrate-binding affinity (Km),...

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Identifiers

PMID: 8954075
DOI: 10.1006/bbrc.1996.1749

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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