4-Aminobutyraldehyde dehydrogenase activity in rat brain.
An enzyme with NAD+-dependent 4-aminobutyraldehyde dehydrogenase activity was purified about 360-fold from rat brain extract. AMP-Sepharose chromatography was effective in separating the enzyme from other NAD+-dependent aldehyde dehydrogenases included in the extract. The KmS for the substrates NAD+ and 4-aminobutyraldehyde were 4.8 x 10(-4) and 8.3 x 10(-5) M, respectively. The pH optimum for the enzyme was about 8.0. The ratio of activities toward 4-aminobutyraldehyde, propionaldehyde, succinate semialdehyde, and benzaldehyde was 1.00:0.17:0.24:0.09:0.03 when the activity toward 4-aminobutyraldehyde was set equal to 1.00. The enzyme activity in subcellular fractions of rat brain was localized in cytosol.
D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000447:Aldehydes / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002082:Butylamines / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D005680:gamma-Aminobutyric Acid / Q000032:analysis
D000447:Aldehydes; D002082:Butylamines; D009243:NAD; D005680:gamma-Aminobutyric Acid; D000445:Aldehyde Oxidoreductases; C019679:aminobutyraldehyde dehydrogenase