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Article

Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase-24.11.

The Journal of biological chemistry - 25 Aug 1991

Le Moual H, Devault A, Roques B P, Crine P, Boileau G

Abstract excerpt

Neutral endopeptidase (EC 3.424.11, NEP) is a membrane-bound zinc-metallopeptidase. The substrate specificity and catalytic activity of NEP resemble those of thermolysin, a bacterial zinc-metalloprotease. Comparison of the primary structure of both enzymes suggests that several amino acids present in the active site of thermolysin are also found in NEP. Using site-directed mutagenesis of the cDNA encoding the NEP...

Topics

Binding Sites
Blotting, Western
Cell Line
Chelating Agents
DNA
Glutamates
Glutamic Acid
Kinetics
Mutagenesis, Site-Directed
Mutation
Neprilysin
Thermolysin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Transfection

Zinc

Source

Identifiers

PMID: 1678740

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1678740-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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