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Article

Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide.

The Journal of biological chemistry - 5 Jul 1991

Johnson J L, Indermaur L W, Rajagopalan K V

Abstract excerpt

The chlorate-resistant mutants of Escherichia coli are affected in the biosynthesis of the molybdenum cofactor and show pleiotropic loss of the activities of those enzymes which require the cofactor. The molybdenum cofactor in all molybdoenzymes other than nitrogenase is a complex of the metal with a unique pterin termed molybdopterin. The molybdenum cofactor in a number of E. coli enzymes has been shown to...

Topics

Chromatography, High Pressure Liquid
Coenzymes
Escherichia coli
Fluorescence Polarization
Guanine Nucleotides
Guanosine Monophosphate
Metalloproteins
Molybdenum Cofactors
Mutation
Pteridines

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Pterins

Pyrophosphatases

Source

Identifiers

PMID: 1648082

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1648082-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide.PMID 1648082Read ↗

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