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Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a
S Setyahadi1, T Ueyama, T Arimoto
1Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Japan.
Bioscience, Biotechnology, and Biochemistry
|June 1, 1997
Abstract:
A new enzyme, D-carnitine dehydrogenase from Agrobacterium sp. 525a, was purified by DEAE-Toyopearl, ammonium sulfate fractionation, Sephadex G-75, affinity chromatography, and Mono Q and TSK-gel filtration column chromatography. The enzyme had the molecular mass of 89 kDa and consisted of three identical subunits. The optimum pH for the oxidation reaction was 9.3. The Michaelis constants for D-carnitine and NAD+ were 3.1 and 0.07 mM, respectively. The N-terminal 20 amino acids were sequenced.