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Article

Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus.

The FEBS journal - 1 Aug 2007

Hershcovitz Yifat F, Gilboa Rotem, Reiland Vera, Shoham Gil, Shoham Yuval

Abstract excerpt

The catalytic mechanism underlying the aminopeptidase from Streptomyces griseus (SGAP) was investigated. pH-dependent activity profiles revealed the enthalpy of ionization for the hydrolysis of leucine-para-nitroanilide by SGAP. The value obtained (30 +/- 5 kJ.mol(-1)) is typical of a zinc-bound water molecule, suggesting that the zinc-bound water/hydroxide molecule acts as the reaction nucleophile. Fluoride was...

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Identifiers

PMID: 17608735
DOI: 10.1111/j.1742-4658.2007.05912.x

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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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