PURIFICATION AND CHARACTERIZATION OF A RAT-BRAIN ALDEHYDE DEHYDROGENASE ABLE TO METABOLIZE GAMMA-AMINOBUTYRALDEHYDE TO GAMMA-AMINOBUTYRIC-ACID

An enzyme which catalyses dehydrogenation of γ-aminobutyraldehyde (ABAL) to γ-aminobutyric acid (GABA) was purified to homogeneity from rat brain tissues by using DEAE-cellulose and affinity chromatography on 5'-AMP-Sepharose, phosphocellulose and Blue Agarose, followed by gel filtration. Such an enzyme was first purified from mammalian brain tissues, and was identified as an isoenzyme of aldehyde dehydrogenase. It has an M(r) of 210000 determined by polyacrylamide-gradient-gel electrophoresis, and appeared to be composed of subunits of M(r) 50000. The close similarity of substrate specificity toward acetaldehyde, propionaldehyde and glycolaldehyde between the enzyme and other aldehyde dehydrogenases previously reported was observed. But substrate specificity of the enzyme toward ABAL was higher than those of aldehyde dehydrogenases from human liver (E1 and E2), and was lower than those of ABAL dehydrogenases from human liver (E3), Escherichia coli and Pseudomonas species. The M(r) and relative amino acid composition of the enzyme are also similar to those of E1 and E2. The existence of this enzyme in mammalian brain seems to be related to a glutamate decarboxylase-independent pathway (alternative pathway) for GABA synthesis from putrescine.