|
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 |
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