Purification and characterization of aminobutyraldehyde dehydrogenase from Arthrobacter Sp. TMP-1

• Published in: Journal of biochemistry, molecular biology and biophysics Vol. 6; no. 3; p. 171
• Main Authors: Tanaka Dagger, Kojiro, Nakai, Ryohsuke, Sen, Kikuo, Shimizu, Eiichi, Karasawa, Den'ei, Yorifuji, Takamitsu
• Format: Journal Article
• Language: English
• Published: England 01.06.2002
• Subjects: Aldehyde Oxidoreductases - chemistry; Aldehyde Oxidoreductases - isolation & purification; Aldehydes - chemistry; Arthrobacter - enzymology; Electrophoresis, Polyacrylamide Gel; Fatty Acids - chemistry; Hydrogen-Ion Concentration; Kinetics; Propylamines - chemistry; Putrescine - chemistry; Substrate Specificity; Temperature
• ISSN: 1025-8140
• DOI: 10.1080/1025814021000000916

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.