Open AccessPurification and characterization of aminopropionaldehyde dehydrogenase from Arthrobacter sp. TMP‐1
Author(s) -
Tanaka Kojiro,
Matsuno Eiji,
Shimizu Eiichi,
Shibai Hiroshiro,
Yorifuji Takamitsu
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10520.x
Subject(s) - nad+ kinase , tetramer , cofactor , molecular mass , dehydrogenase , chemistry , enzyme , stereochemistry , oxidoreductase , arthrobacter , michaelis–menten kinetics , biochemistry , enzyme assay
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 205 000 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 μM. The enzyme equally used both NAD + and NADP + as coenzymes. The apparent K m values for NAD + and NADP + were 255 μM and 108 μM, respectively. The maximum reaction rates ( V max ) for NAD + and NADP + were 102 and 83.3 μmol 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.