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Article

Oxidized and Met358-->Leu mutated alpha 1-proteinase inhibitor as substrates of Pseudomonas aeruginosa elastase.

Biochimica et biophysica acta - 21 Apr 1993

Padrines M, Bieth J G

Abstract excerpt

This paper investigates the catalytic activity of Pseudomonas aeruginosa elastase using the bait region of the alpha 1-proteinase inhibitor as a substrate. The bacterial enzyme cleaves the Pro357-Met358 bond of the wild-type inhibitor and the recombinant Met358 inhibitor and the Pro357-Leu358 bond of the recombinant Met358-->Leu inhibitor with kcat/Km values of 9 x 10(4) M-1 s-1, 1.4 x 10(5) M-1 s-1 and 3.5 x...

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Topics

Amino Acid Sequence
Hydrogen-Ion Concentration
Kinetics
Leucine
Methionine
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Oxidation-Reduction

Pancreatic Elastase

Protease Inhibitors

Pseudomonas aeruginosa

Recombinant Proteins

Substrate Specificity

Source

Identifiers

PMID: 8476930
DOI: 10.1016/0167-4838(93)90279-z

Provenance

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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