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J Bacteriol. 1967 October; 94(4): 1034-1039
Copyright © 1967 American Society for Microbiology. All Rights Reserved.
a Department of Biochemistry, School of Medicine, University of California, San Francisco Medical Center, San Francisco, California 94122
ABSTRACT
Oxidation of pipecolate to
1-piperideine-6-carboxylate is catalyzed by pipecolate oxidase, an inducible, membrane-bound dehydrogenase associated with the electron transport components of Pseudomonas putida P2. From the oxidase, we obtained a smaller particle containing flavine adenine dinucleotide (FAD) and cytochrome b, but no longer able to catalyze electron transfer to oxygen or to cytochrome c. Certain properties of this L-pipecolate dehydrogenase, an FAD-flavoprotein, are reported.
1 Present address: Division of Biochemistry, Scripps Clinic and Research Foundation, La Jolla, Calif. 92037.
2 Present address: Department of Biochemistry, Purdue University, Lafayette, Ind. 47907.
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