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A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely r...

A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely r...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1865377

A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase

About this item

Full title

A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase

Publisher

England: BioMed Central Ltd

Journal title

BMC biochemistry, 2007-04, Vol.8 (1), p.4-4, Article 4

Language

English

Formats

Publication information

Publisher

England: BioMed Central Ltd

More information

Scope and Contents

Contents

In microorganisms and plants, the first two reactions of arginine biosynthesis are catalyzed by N-acetylglutamate synthase (NAGS) and N-acetylglutamate kinase (NAGK). In mammals, NAGS produces an essential activator of carbamylphosphate synthetase I, the first enzyme of the urea cycle, and no functional NAGK homolog has been found. Unlike the other...

Alternative Titles

Full title

A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1865377

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1865377

Other Identifiers

ISSN

1471-2091

E-ISSN

1471-2091

DOI

10.1186/1471-2091-8-4

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