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Article

Characterization and rational design for substrate specificity of a prolyl endopeptidase from Stenotrophomonas maltophilia.

Enzyme and microbial technology - 1 Aug 2020

Yu Junjie, Wu Junjie, Xie Dewei, Du Lei, Tang Ya-Jie, Xie Jingli, Wei Dongzhi

Abstract excerpt

A novel prolyl endopeptidase from Stenotrophomonas maltophilia, SmPEP, was discovered and characterized. The specific activity of the recombinant SmPEP expressed by Escherichia coli BL21 (DE3), was 68.3 U/mg at pH 8.0 and 37 °C. In order to improve the substrate specificity for long-chain peptide, rational design was applied based on the structure constructed by homology modeling. Inter-domain sites within the...

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PMID: 32527522
DOI: 10.1016/j.enzmictec.2020.109548

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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