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Article

A functional analysis of the allosteric nucleotide monophosphate binding site of carbamoyl phosphate synthetase.

Archives of biochemistry and biophysics - 1 Apr 2002

Pierrat Olivier A, Raushel Frank M

Abstract excerpt

The catalytic activity of carbamoyl phosphate synthetase (CPS) from Escherichia coli is allosterically regulated by UMP, IMP, and ornithine. Thirteen amino acids within the domain that harbors the overlapping binding sites for IMP and UMP were mutated to alanine and characterized. The four residues that interact directly with the phosphate moiety of IMP in the X-ray crystal structure (K954, T974, T977, and K993)...

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Identifiers

PMID: 11913968
DOI: 10.1006/abbi.2002.2767

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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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