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B6db references: 76210291

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
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

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