Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.

نویسندگان

  • J S Holcenberg
  • E R Stadtman
چکیده

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 triphosphopyridine nucleotide oxidase and diaphorase activity.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 244 5  شماره 

صفحات  -

تاریخ انتشار 1969