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Article

The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.

Biochimica et biophysica acta - 10 Nov 1998

Hewagama A, Guy H I, Chaparian M, Evans D R

Abstract excerpt

The synthesis of carbamoyl phosphate by the mammalian multifunctional protein, CAD, involves the concerted action of the 40 kDa amidotransferase domain (GLN), that hydrolyzes glutamine and the 120 kDa synthetase (CPS) domain that uses the ammonia, thus produced, ATP and bicarbonate to make carbamoyl phosphate. The separately cloned GLN domain has very low activity due to a reduction in kcat and an increase in Km...

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Source

Identifiers

PMID: 9858783
DOI: 10.1016/s0167-4838(98)00212-x

Genes

CAD

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.PMID 9858783Read ↗

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Access to the carbamate tunnel of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Interdomain signaling in glutamine phosphoribosylpyrophosphate amidotransferase.Semantic proximity Read ↗

Human carbamoyl-phosphate synthetase: insight into N-acetylglutamate interaction and the functional effects of a common single nucleotide polymorphism.Semantic proximity Read ↗

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