Purification and characterization of aminopropionaldehyde dehydrogenase from Arthrobacter sp. TMP-1.
Aminopropionaldehyde dehydrogenase was purified to apparent homogeneity from 1,3-diaminopropane-grown cells of Arthrobacter sp. TMP-1. The native molecular mass and the subunit molecular mass of the enzyme were approximately 20,5000 and 52,000, respectively, suggesting that the enzyme is a tetramer of identical subunits. The apparent Michaelis constant (K(m)) for 1,3-diaminopropane was approximately 3 microM. The enzyme equally used both NAD(+) and NADP(+) as coenzymes. The apparent K(m) values for NAD(+) and NADP(+) were 255 microM and 108 microM, respectively. The maximum reaction rates (V(max)) for NAD(+) and NADP(+) were 102 and 83.3 micromol min(-1) mg(-1), respectively. Some tested aliphatic aldehydes and aromatic aldehydes were inert as substrates. The optimum pH was 8.0-8.5. The enzyme was sensitive to sulfhydryl group-modifying reagents.
Tanaka
K
K
Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University, 8304 Minamiminowa, Nagano 399-4598, Japan. tanakak@gipmc.shinsu-u.ac.jp
Matsuno
E
E
Shimizu
E
E
Shibai
H
H
Yorifuji
T
T
D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D001173:Arthrobacter / Q000201:enzymology*; D003959:Diamines / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004794:Enzyme Repression; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D021122:Protein Subunits; D013379:Substrate Specificity; D013696:Temperature; D020245:p-Chloromercuribenzoic Acid / Q000494:pharmacology
D000447:Aldehydes; D003959:Diamines; D004791:Enzyme Inhibitors; D021122:Protein Subunits; D009243:NAD; D009249:NADP; D020245:p-Chloromercuribenzoic Acid; C009475:trimethylenediamine; D000445:Aldehyde Oxidoreductases; C428003:aminopropioaldehyde dehydrogenase