Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a

被引：7
|
作者：
Setyahadi, S
Ueyama, T
Arimoto, T
Mori, N
Kitamoto, Y
机构：
[1] Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Tottori
来源：
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1997年 / 61卷 / 06期
关键词：
D-carnitine dehydrogenase; degradation of D-carnitine;
D O I：
10.1271/bbb.61.1055
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1055 / 1058
页数：4
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