|
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 |
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