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Article

Dissection of the conduit for allosteric control of carbamoyl phosphate synthetase by ornithine.

Archives of biochemistry and biophysics - 1 Apr 2002

Pierrat Olivier A, Javid-Majd Farah, Raushel Frank M

Abstract excerpt

Ornithine is an allosteric activator of carbamoyl phosphate synthetase (CPS) from Escherichia coli. Nine amino acids in the vicinity of the binding sites for ornithine and potassium were mutated to alanine, glutamine, or lysine. The residues E783, T1042, and T1043 were found to be primarily responsible for the binding of ornithine to CPS, while E783 and E892, located within the carbamate domain of the large...

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Identifiers

PMID: 11913967
DOI: 10.1006/abbi.2002.2768

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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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