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Article

Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural and recombinant variants of cystatins and stefins.

Biomedica biochimica acta - 1 Jan 1991

Machleidt W, Thiele U, Assfalg-Machleidt I, Förger D, Auerswald E A

Abstract excerpt

Natural and recombinant variants of the cysteine proteinase inhibitors chicken cystatin and human stefin B were characterized by determination of their inhibition constants for papain, actinidin and human cathepsins B and H. The individual contributions of the three contact regions to the binding energy of the chicken cystatin-papain complex were calculated as 36% for the N-terminal segment, 51% for the first and...

Topics

Amino Acid Sequence
Animals
Binding Sites
Cathepsin B
Cathepsin H
Cathepsins
Cystatin B
Cystatins
Cysteine Endopeptidases
Genetic Variation
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

In Vitro Techniques

Kinetics

Molecular Sequence Data

Papain

Source

Identifiers

PMID: 1801731

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1801731-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural and recombinant variants of cystatins and stefins.PMID 1801731Read ↗

Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain.Semantic proximity Read ↗

Contributions of individual residues in the N-terminal region of cystatin B (stefin B) to inhibition of cysteine proteinases.Semantic proximity Read ↗

The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.Semantic proximity Read ↗

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