Purification and properties of betaine aldehyde dehydrogenase with high affinity for NADP from Arthrobacter globiformis.
Betaine aldehyde dehydrogenase from Arthrobacter globiformis was purified to apparent homogeneity by ammonium sulfate fractionation, followed by ion-exchange, butyl-Toyopearl and gel filtration chromatography. The enzyme was found to be a tetramer with identical 55 kDa subunits. Both NAD+ and NADP+ could be used as a cofactor for the enzyme and Michaelis constants (K(m) value) for NAD+ and NADP+ were 1075 microM and 48 microM, respectively. The enzyme was highly specific for betaine aldehyde and the K(m) value for betaine aldehyde was 36 microM.
Mori
Nobuhiro
N
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, 4-101 Koyama-cho Minami, Tottori 680-8553, Japan. morinobu@muses.tottori-u.ac.jp
Fuchigami
Sayuri
S
Kitamoto
Yutaka
Y