type	Journal Article
authors	Sukanya, N. K.; Vaidyanathan, C. S.
title	Tryptophan-phenylpyruvate aminotransferase of Agrobacterium tumefaciens: purification and general properties of the enzyme
journal	J Ind Inst Sci
Activity	2.6.1.28
ui	frhSxiFnd
year	(1979)
volume	61
number	12
pages	51-62
keywords	Agrobacterium/*enzymology
abstract	Tryptophan-phenylalanine aminotransferase (I) of A. tumefaciens was purified 67.5-fold with a yield of 90% from crude exts. and characterized. I had a pH optimum of 9.6 and showed significant activity at pH 10.6. The optimum temp. was 50°, with complete inactivation at 70°. This thermostability was increased in the presence of substrates of pyridoxal 5'-phosphate (II), the order of protection against heat denaturation being II > phenylpyruvate > tryptophan. I activity increased with increasing protein concn. from 10 to 100 mg.
last changed	2007/11/14 14:44