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Article

Probing cathepsin K activity with a selective substrate spanning its active site.

The Biochemical journal - 15 Oct 2003

Lecaille Fabien, Weidauer Enrico, Juliano Maria A, Brömme Dieter, Lalmanach Gilles

Abstract excerpt

The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine proteases, cathepsin K has a unique preference for a proline residue at P2, the primary determinant of its substrate specificity. Interestingly, congopain from Trypanosoma congolense also accommodates a proline residue in...

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Identifiers

PMID: 12837132
DOI: 10.1042/BJ20030468
PMCID: PMC1223680

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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