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Article

Cloning, expression, and functional interactions of the amidotransferase domain of mammalian CAD carbamyl phosphate synthetase.

The Journal of biological chemistry - 11 Mar 1994

Guy H I, Evans D R

Abstract excerpt

The trpG-type amidotransferases, a homologous but structurally diverse family of molecules, catalyze glutamine hydrolysis to supply ammonia for many biosynthetic reactions. The amidotransferase or glutaminase (GLNase) domain of mammalian carbamyl phosphate synthetase (CPSase), part of a 243-kDa polypeptide that initiates de novo pyrimidine biosynthesis, has been cloned and expressed in Escherichia coli....

Topics

Animals
Aspartate Carbamoyltransferase
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Cloning, Molecular
Cricetinae
Dihydroorotase
Escherichia coli
Genetic Complementation Test
Glutaminase
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mesocricetus

Multienzyme Complexes

Mutation

Recombinant Proteins

Source

Identifiers

PMID: 7907330

Genes

CAD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7907330-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Cloning, expression, and functional interactions of the amidotransferase domain of mammalian CAD carbamyl phosphate synthetase.PMID 7907330Read ↗

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