descriptionPublicationkeyboard_double_arrow_right Article 01 May 1974 English Publisher:Canadian Science PublishingJournal:Canadian Journal of Microbiology, volume 20, pages 695-702 (issn: 0008-4166, eissn: 1480-3275,

Authors: R. L. Tate; J. C. Ensign;

doi: 10.1139/m74-106

pmid: 4832254

Picolinic acid hydroxylase of Arthrobacter picolinophilus

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Abstract

Picolinic acid is oxidized by cells and extracts of Arthrobacter picolinophilus to 6-hydroxypicolinic acid. The enzyme involved is a particulate hydroxylase which appears to incorporate the hydroxyl group of water into the substrate. The enzyme was purified about 60-fold. The molecular weight as determined by gel filtration was 230 000 daltons. Activity of the purified enzyme was stimulated by ferrous ions and was inhibited by quinacrine. Flavin mononucleotide reversed the inhibition by quinacrine.

Keywords

Spectrophotometry, Infrared, Flavin Mononucleotide, Iron, Hydrogen-Ion Concentration, Electrophoresis, Disc, Hydroxylation, Mixed Function Oxygenases, Molecular Weight, Oxygen Consumption, Quinacrine, Chromatography, Gel, Spectrophotometry, Ultraviolet, Arthrobacter, Picolinic Acids

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