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Article

The effect of changing the hydrophobic S1' subsite of thermolysin-like proteases on substrate specificity.

European journal of biochemistry - 1 Sept 2001

de Kreij A, van den Burg B, Veltman O R, Vriend G, Venema G, Eijsink V G

Abstract excerpt

The hydrophobic S1' subsite is one of the major determinants of the substrate specificity of thermolysin and related M4 family proteases. In the thermolysin-like protease (TLP) produced by Bacillus stearothermophilus (TLP-ste), the hydrophobic S1' subsite is mainly formed by Phe130, Phe133, Val139 and Leu202. In the present study, we have examined the effects of replacing Leu202 by smaller (Gly, Ala, Val) and...

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Identifiers

PMID: 11559368
DOI: 10.1046/j.0014-2956.2001.02434.x

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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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