Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.
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.
Kanda
M
M
Department of Biochemistry, Hyogo College of Medicine, Nishinomiya, Japan.
Hori
K
K
Kurotsu
T
T
Ohgishi
K
K
Hanawa
T
T
Saito
Y
Y
D001407:Bacillus / Q000201:enzymology* / Q000378:metabolism*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006096:Gramicidin / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D011732:Pyridoxal Phosphate / Q000032:analysis; D013053:Spectrophotometry; D013379:Substrate Specificity; D000637:Transaminases / Q000737:chemistry / Q000302:isolation & purification*
D006096:Gramicidin; D011732:Pyridoxal Phosphate; D000637:Transaminases; C019798:branched-chain-amino-acid transaminase