PMID:9573170
| Citation |
Suvarna, K, Stevenson, D, Meganathan, R and Hudspeth, ME (1998) Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 180:2782-7 |
|---|---|
| Abstract |
A key reaction in the biosynthesis of menaquinone involves the conversion of the soluble bicyclic naphthalenoid compound 1, 4-dihydroxy-2-naphthoic acid (DHNA) to the membrane-bound demethylmenaquinone. The enzyme catalyzing this reaction, DHNA-octaprenyltransferase, attaches a 40-carbon side chain to DHNA. The menA gene encoding this enzyme has been cloned and localized to a 2.0-kb region of the Escherichia coli genome between cytR and glpK. DNA sequence analysis of the cloned insert revealed a 308-codon open reading frame (ORF), which by deletion analyses was shown to restore anaerobic growth of a menA mutant. Reverse-phase high-performance liquid chromatography analysis of quinones extracted from the orf-complemented cells independently confirmed the restoration of menaquinone biosynthesis, and similarly, analyses of isolated cell membranes for DHNA octaprenyltransferase activity confirmed the introduction of the menA product into the orf-complemented menA mutant. The validity of an ORF-associated putative promoter sequence was confirmed by primer extension analyses. |
| Links | |
| Keywords |
Alkyl and Aryl Transferases/genetics; Alkyl and Aryl Transferases/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Molecular Sequence Data; Naphthols/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Vitamin K/biosynthesis |
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