type	Journal Article
authors	Van Leuven, F.
title	Glutamine transaminase from brain tissue. Further studies on kinetic properties and specificity of the enzyme
journal	Eur J Biochem
Activity	2.6.1.64
ui	76210291
year	(1976)
volume	65
number	1
pages	271-4.
keywords	Amino Acids
abstract	Glutamine transaminase, highly purified from rat brain, was studied. In the first series of experiments, the kinetics of the transamination reaction between 2-oxoglutaramate and phenylalanine were examined in order to determine the type of reaction mechanism. This proved to be of the ping-pont type, as can be expected for a transamination. The specificity of the enzyme for various amino acids and 2-oxo acids was then studied in detail. The most active substrates were glutamine, methionine and ethionine as amino-group donors, and phenylpyruvate, glyoxalate and 2-oxo-4-methiobutyrate as amino-group acceptors. For these and several other substrates, the kinetic constants, V and Km, were determined.
last changed	2002/11/02 00:35