Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis

• Published in: Journal of Nutritional Science and Vitaminology 1995, Vol.41(1), pp.51-60
• Main Authors: Kanda, M. (Hyogo Coll. of Medicine, Nishinomiya (Japan)), Hori, K, Kurotsu, T, Ohgishi, K, Hanawa, T, Saito, Y
• Format: Article
• Language: English
• Subjects: AMINOTRANSFERASAS; AMINOTRANSFERASE; AMINOTRANSFERASES; ANTIBIOTICOS; ANTIBIOTICS; ANTIBIOTIQUE; BACILLUS; Bacillus - enzymology; Bacillus - metabolism; Bacillus brevis; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; branched chain amino acid aminotransferase; Chromatography; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Fundamental and applied biological sciences. Psychology; Gramicidin - metabolism; Gramicidin S; Hydrogen-Ion Concentration; Isoelectric Point; Mission oriented research; Molecular Weight; Physiology and metabolism; PIRIDOXINA; PURIFICACION; PURIFICATION; pyridoxal phosphate; Pyridoxal Phosphate - analysis; PYRIDOXINE; Spectrophotometry; Substrate Specificity; Transaminases - chemistry; Transaminases - isolation & purification
• ISSN: 0301-4800; 1881-7742
• DOI: 10.3177/jnsv.41.51

The branched chain amino acid aminotransferase [EC 2.6.1.42] was purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. The enzyme had a molecular weight of about 93, 000 and consisted of two identical subunits, each with a molecular weight of about 47, 000. One pyridoxal phosphate is bound per subunit. In addition to branched chain amino acids, the enzyme uses L-phenylalanine and L-tryptophan as the amino donor, indicating that B. brevis branched chain amino acid aminotransferase has a broad substrate specificity for the amino donor. The enzyme utilized 2-oxoglutarate as the amino acceptor. The purified enzyme exhibits its absorption maxima at 332 and 427 nm at neutral pH.