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Article

Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group.

Archives of biochemistry and biophysics - 15 Oct 2004

Carvajal Nelson, Orellana María S, Salas Mónica, Enríquez Paula, Alarcón Ricardo, Uribe Elena, López Vasthi

Abstract excerpt

The interaction of Escherichia coli agmatinase (EC 3.5.3.11) with the substrate guanidinium group was investigated by kinetic and site-directed mutagenesis studies. Putrescine and guanidinium ions (Gdn+) were slope-linear, competitive inhibitors with respect to agmatine and their bindings to the enzyme were not mutually exclusive. By site-directed mutagenesis, the E274A variant exhibiting about 1-2% of wild-type...

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Identifiers

PMID: 15369817
DOI: 10.1016/j.abb.2004.07.005

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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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