Distribution of omega amino acid pyruvate trans aminase ec 184.108.40.206 and amino butyrate alpha keto glutarate trans aminase ec 220.127.116.11 in microorganisms
Yonaha, K.; Suzuki, K.; Minei, H.; Toyama, S.
Agricultural and Biological Chemistry 47(10): 2257-2266
ISSN/ISBN: 0002-1369 Accession: 005179502
The distribution of .omega.-amino acid transaminases in microorganisms was investigated. .omega.-Amino acid:pyruvate transaminase (.omega.-APT) was found in bacteria and yeasts, but not in actinomycetes and fungi. Aminobutyrate: .alpha.-ketoglutarate transaminase (GABA-T) was shown in most of the microorganisms from bacteria to fungi. .beta.-Alanine was a preferred amino donor for the .omega.-APT reaction. Although bacterial and yeast GABA-T were inactive for .beta.-alanine, fungal and actinomycete enzymes reacted with this compound and GABA. In comparing these results with those of plant and mammalian enzymes, 2 different pathways of .omega.-amino acid metabolism are suggested for bacteria, yeast and plants, i.e., one for .beta.-alanine and the other for GABA, catalyzed by .omega.-APT and GABA-T, respectively. In actinomycetes, fungi and mammals, GABA-T may be involved in the metabolism of both .omega.-amino acids. Evolutionary changes of .omega.-amino acid transaminases are discussed.