Activities | Families | Sequences | Fold types | References | Help
B6db references: frhsxifnd

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
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

B6db references