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B6db references: 95341416

type Journal Article
authors Kanda, M.; Hori, K.; Kurotsu, T.; Ohgishi, K.; Hanawa, T.; Saito, Y.
title Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis
journal J Nutr Sci Vitaminol (Tokyo)
Activity 2.6.1.42
ui 95341416
year (1995)
volume 41
number 1
pages 51-60.
 
keywords Bacillus/*enzymology/*metabolism
abstract 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.
last changed 2002/11/12 16:17

B6db references