Purification and characterization of aminobutyraldehyde dehydrogenase from Arthrobacter Sp. TMP-1.
Aminobutyraldehyde dehydrogenase was purified to essentially homogeneity from putrescine-grown cells of Arthrobacter sp. TMP-1. The molecular weights of the enzyme and its subunit were 201,000 and 51,000, respectively, suggesting that the enzyme is a tetramer of identical subunits. The apparent Michaelis constants (K(m)) for 4-aminobutyraldehyde, 3-aminopropionaldehyde and 4-guanidinobutyraldehyde were approximately 65, 150, and 85 microM, respectively. Linear fatty aldehydes also tested were less active as a substrate, while the tested succinate-semialdehyde and branched fatty aldehydes were inert. The enzyme utilized both NAD(+) and NADP(+) as coenzymes. The optimum pH was 8.0. The enzyme lost 64% of its activity when held at 40 degrees C for 10 min.
Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University, Minamiminowa, Nagano, Japan. tanakak@gipmc.shinshu-u.ac.jp
Kojiro
K
Tanaka Dagger
Ryohsuke
R
Nakai
Kikuo
K
Sen
Eiichi
E
Shimizu
Den'ei
D
Karasawa
Takamitsu
T
Yorifuji
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification*; D000447:Aldehydes / Q000737:chemistry; D001173:Arthrobacter / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011437:Propylamines / Q000737:chemistry; D011700:Putrescine / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature
D000447:Aldehydes; D005227:Fatty Acids; D011437:Propylamines; C006509:4-aminobutyraldehyde; D000445:Aldehyde Oxidoreductases; C019679:aminobutyraldehyde dehydrogenase; C018475:butyraldehyde; C050862:3-aminopropionaldehyde; D011700:Putrescine