Oxidation of Nicotinic Acid by a Bacillus Species: Purification and Properties of Nicotinic Acid and 6-Hydroxynicotinic Acid Hydroxylases
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چکیده
منابع مشابه
Oxidation of nicotinic acid by a Bacillus species: purification and properties of nicotinic acid and 6-hydroxynicotinic acid hydroxylases.
The enzymes of a Bacillus species that hydroxylate nicotinic acid to 6-hydroxynicotinic acid and 6-hydroxynicotinic acid to 2,6-dihydroxynicotinic acid were purified and characterized. The purified enzymes contained approximately two molecules of flavine and eight molecules of iron per molecule of enzyme. The enzymes were large (molecular weight, 400,000 to 450,000) and appeared to consist of s...
متن کاملOxidation of nicotinic acid by a Bacillus species: regulation of nicotinic acid and 6-hydroxynicotinic acid hydroxylases.
The first two enzymes employed by a Bacillus species for the dissimilation of nicotinic acid are coordinately induced. The inducer of the enzymes appears to be 6-hydroxynicotinic acid, the product of the first enzyme in the pathways. Synthesis of the enzymes is repressed by glucose when ammonium is present in the medium, but not when nicotinic acid is the sole nitrogen source. The possible sign...
متن کاملOxidation of nicotinic acid by a Bacillus species: source of oxygen atoms for the hydroxylation of nicotinic acid and 6-hydroxynicotinic acid.
Three types of evidence are presented to show that the enzymes that hydroxylate nicotinic acid to 2,6-dihydroxynicotinic acid use water as a source of oxygen atoms. (18)O is incorporated into the products from H(2) (18)O. Molecular oxygen acts as a terminal electron acceptor, one-half molecule being consumed per molecule of hydroxyl groups incorporated. An external electron acceptor is required...
متن کاملThe Pathway of Nicotinic Acid Oxidation by a Bacillus Species.
Bacteria able to grow with nicotinic acid as a sole source of carbon and nitrogen have been isolated by a number of investigators (l-5). Hughes et al. (6-10) found that Pseudomonas jlzwrescens initiates degradation of nicotinic acid by a hydroxylation to form 6-hydroxynicotinic acid and established that the responsible enzyme is located in a cell wall membrane fraction. An initial hydroxylation...
متن کاملNicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.
An enzyme that catalyzes the reversible hpdroxylation of nicotinic acid to 6-hydroxynicotinic acid has been purified from extracts of a nicotinic acid-fermenting clostridium. The enzyme appears to be a flavin adenine dinucleotidecontaining non-heme iron protein and utilizes triphosphopyridine nucleotide as the ultimate electron acceptor. The purified enzyme also exhibits reduced triphosphopyrid...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1971
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.108.2.751-756.1971