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Article

Role of a disulphide bond in Helicobacter pylori arginase.

Biochemical and biophysical research communications - 7 May 2010

Srivastava Abhishek, Dwivedi Nidhi, Sau Apurba Kumar

Abstract excerpt

Arginase is a binuclear Mn(2+)-metalloenzyme of urea cycle that hydrolyses arginine to ornithine and urea. Unlike other arginases, the Helicobacter pylori enzyme is selective for Co(2+). Previous study reported that DTT strongly inhibits the H. pylori enzyme activity suggesting that a disulphide bond is critical for the catalysis. In this study, we have undertaken steady-state kinetics, circular dichroism and...

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Source

Identifiers

PMID: 20381458
DOI: 10.1016/j.bbrc.2010.04.014

Provenance

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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