Induction of D-6-hydroxynicotine oxidase in resting cells of Arthrobacter oxidans.

Resting cell suspensions of Arthrobacter oxidans were shown to synthesize the inducible enantiozyme, D-6-hydroxynicotine oxidase, in the presence of D-nicotine or D-6-hydroxynicotine. The corresponding L-enantiomers, as well as gamma-methylaminopropyl-(6-OH-pyridyl-3)-ketone, which is the product of the reaction catalyzed by the enzyme, were ineffective as inducers. L-6-Hydroxynicotine inhibited induction by D-nicotine and D-6-hydroxynicotine while L-nicotine inhibited induction by D-6-hydroxynicotine and had no effect on induction by D-nicotine. Enzyme induction was also found to be inhibited by glucose, 2-deoxy-D-glucose and by several intermediates of the tricarboxylic acid cycle. An absolute requirement for protein synthesis and for oxygen was also demonstrated to be necessary for the reactions involved in the covalent attachment of flavin adenine dinucleotide to pre-existing precursor protein to yield the catalytically active D-6-hydroxynicotine oxidase.