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Article

pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15).

FEBS letters - 19 Jun 2003

Sigman Jeffrey A, Edwards Sarah R, Pabon Amanda, Glucksman Marc J, Wolfson Adele J

Abstract excerpt

Thimet oligopeptidase (EC 3.4.24.15; TOP) is a Zn(II) endopeptidase implicated in physiological regulation of processes involving neuropeptides. The present study clarifies the active site structure and mechanism of catalysis of TOP. The enzyme exhibited a bell-shaped pH dependence of activity having an acidic limb due to a protonation event with a pK(a) of 5.7 and a basic limb with pK(a) of 8.8. The acidic limb...

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Identifiers

PMID: 12804780
DOI: 10.1016/s0014-5793(03)00548-9

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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