|
type |
Journal Article |
authors |
Sukanya, N. K.; Vaidyanathan, C. S. |
title |
Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate |
journal |
Biochem J |
Activity |
2.6.1.28 |
ui |
66031006 |
year |
(1964) |
volume |
92 |
number |
3 |
pages |
594-8. |
| |
keywords |
Agrobacterium/*enzymology |
abstract |
1. Evidence is presented to show that the first step involved in the conversion of tryptophan into indolylacetic acid by Agrobacterium tumefaciens involves transamination.
2. A 68-fold purification of an aminotransferase, exhibiting a broad specificity with comparable transaminase activities with tryptophan, valine, leucine and isoleucine as amino donors and phenylpyruvate as acceptor, was achieved.
3. The optimum pH for the enzyme activity is 9-6. The activity at higher pH values, though less than optimurn, is significant.
4. Substrates and pyridoxal phosphate stabilize the enzyme against thermal denaturation. |
last changed |
2007/11/14 14:50 |
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