PMID:2666397
| Citation |
Popp, JL (1989) Sequence and overexpression of the menD gene from Escherichia coli. J. Bacteriol. 171:4349-54 |
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| Abstract |
The menD gene of Escherichia coli codes for the first enzyme of menaquinone biosynthesis, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase. DNA sequence analysis of menD shows an open reading frame encoding a 52-kilodalton protein. Possible promoter and ribosome binding sites are present. Insertion of the menD gene into a tac promoter expression vector leads to nearly a 100-fold increase in the level of SHCHC synthase activity upon induction with isopropyl-beta-D-thiogalactoside (IPTG). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of [35S]methionine-labeled proteins shows a 61-kilodalton protein produced upon induction of the menD-containing expression vector. This is the first reported sequence analysis of a men gene and the first significant amplification of any of the menaquinone biosynthetic enzymes. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression Regulation; Genes; Genes, Bacterial; Genotype; Molecular Sequence Data; Oxo-Acid-Lyases/genetics; Oxo-Acid-Lyases/metabolism; Restriction Mapping; Species Specificity |
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