Anaerobic biosynthesis of enterobactin Escherichia coli: regulation of entC gene expression and evidence against its involvement in menaquinone (vitamin K2) biosynthesis
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منابع مشابه
Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menE gene from Escherichia coli.
In Escherichia coli, the biosynthesis of the electron carrier menaquinone (vitamin K2) involves at least seven identified enzymatic activities, five of which are encoded in the men cluster. One of these, the conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid, requires the formation of o-succinylbenzoyl-CoA (OSB-CoA) as an intermediate. Formation of the intermediate is mediat...
متن کاملMenaquinone (vitamin K2) biosynthesis: overexpression, purification, and characterization of a new isochorismate synthase from Escherichia coli.
The first committed step in the biosynthesis of menaquinone (vitamin K2) is the conversion of chorismate to isochorismate, which is mediated by an isochorismate synthase encoded by the menF gene. This isochorismate synthase (MenF) is distinct from the entC-encoded isochorismate synthase (EntC) involved in enterobactin biosynthesis. MenF has been overexpressed under the influence of the T7 promo...
متن کاملBiosynthesis of Menaquinone (Vitamin K2) and Ubiquinone (Coenzyme Q).
Escherichia coli and Salmonella contain the naphthoquinones menaquinone (MK; vitamin K2) and demethylmenaquinone and the benzoquinone ubiquinone (coenzyme Q; Q). Both quinones are derived from the shikimate pathway, which has been called a "metabolic tree with many branches." There are two different pathways for the biosynthesis of the naphthoquinones. The vast majority of prokaryotes, includin...
متن کاملVitamin K2 (menaquinone) biosynthesis in Escherichia coli: evidence for the presence of an essential histidine residue in o-succinylbenzoyl coenzyme A synthetase.
o-Succinylbenzoyl coenzyme A (OSB-CoA) synthetase, when treated with diethylpyrocarbonate (DEP), showed a time-dependent loss of enzyme activity. The inactivation follows pseudo-first-order kinetics with a second-order rate constant of 9.2 x 10(-4) +/- 1.4 x 10(-4) microM(-1) min(-1). The difference spectrum of the modified enzyme versus the native enzyme showed an increase in A242 that is char...
متن کاملo-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis, displays broad specificity.
o-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone biosynthesis, was purified from Mycobacterium phlei and characterized with respect to isoelectric point, molecular weight, pH optimum, temperature optimum and kinetic data. The enzyme hydrolyses ATP to AMP. The substrate and cofactor specificity of the enzyme was tested with analogues of o-succinylbenzoic acid, different n...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1996
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.178.11.3252-3259.1996