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Article

Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli.

European journal of biochemistry - 1 Jun 1994

Palmer T, Vasishta A, Whitty P W, Boxer D H

Abstract excerpt

The mob mutants in Escherichia coli are pleiotropically defective in all molybdoenzyme activities. They synthesise molybdopterin, the unique core of the molybdenum cofactor, but are unable to attach the GMP moiety to molybdopterin to form molybdopterin guanine dinucleotide, the functional molybdenum cofactor in Escherichia coli. A partially purified preparation termed protein FA (protein factor d'association), is...

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Identifiers

PMID: 8020507
DOI: 10.1111/j.1432-1033.1994.tb18913.x

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

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