Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a.
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.
Setyahadi
S
S
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Japan.
Ueyama
T
T
Arimoto
T
T
Mori
N
N
Kitamoto
Y
Y
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000187:drug effects / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D000645:Ammonium Sulfate / Q000737:chemistry; D005591:Chemical Fractionation; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D012231:Rhizobium / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D008670:Metals; D000429:Alcohol Oxidoreductases; C019842:carnitine dehydrogenase; D000645:Ammonium Sulfate