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 sub-units. 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 muM and 48 muM, respectively. The enzyme was highly specific for betaine aldehyde and the K-m value for betaine aldehyde was 36 muM.