D-6-Hydroxynicotine oxidase

L-Nicotine oxidation by cell-free extracts of Arthrobacter oxydans yields L-6-hydroxynicotine exclusively. When Arthrobacter oxydans is grown on DL-nicotine, l- and d-6-hydroxynicotine oxidases are produced and have been separated. L-6-Hydroxynicotine oxidase converts L-6-hydroxynicotine to 5-(7-methylaininobutyryl)-2-pyridone (XI1.841) in the presence of oxygen by a mechanism that consists of dehydrogenation followed by hydrolysis of the intermediate enamine (XII-840). ... 

Since this work was done, 8a-N(3)-histidyl-FAD cf. 9a) has been identified in D-6-hydroxynicotine oxidase from Arthrobacter oxidans 10, 11, 131). It is probably also present in sarcosine dehydrogenase from pseudomonas 143) and from rat liver 144), and is possibly also the coenzyme of dimethylglycine dehydrogenase from rat liver 37). 

Bruhmuller, M., and K. Decker Covalently Bound Flavin in D-6-Hydroxynicotine Oxidase from Arthrobacter oxidans. Amino-Acid Sequence of the FAD-Peptide. Eur. J. Biochem. 37, 256 (1973). 

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See also in sourсe #XX -- [ ]

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