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