|
type |
Journal Article |
authors |
Tamaki, N.; Fujimoto, S.; Mizota, C.; Kikugawa, M. |
title |
Identity of beta-alanine-oxo-glutarate aminotransferase and L-beta- aminoisobutyrate aminotransferase in rat liver |
journal |
Biochim Biophys Acta |
Activity |
2.6.1.19 |
Family |
2.6.1.19.a |
sel |
selected |
ui |
3113494 |
year |
(1987) |
volume |
925 |
number |
2 |
pages |
238-40 |
| |
keywords |
Aminoisobutyric Acids/metabolism |
abstract |
L-beta-Aminoisobutyrate served as an amino donor for purified beta- alanine-oxo-glutarate aminotransferase from rat liver when 2- oxoglutarate was employed as an amino acceptor, but the D-isomer did not. L-beta-Aminoisobutyrate acted as a competitive inhibitor with respect to beta-alanine and had a Ki of approximately 2.6 mM, which is the same value as the Km of 2.7 mM. When the crude extract was applied to a DEAE-Sepharose CL-6B column, L-beta-aminoisobutyrate aminotransferase and beta-alanine-oxo-glutarate aminotransferase activities were found in the same fractions with a single peak. Antiserum to rat liver beta-alanine-oxo-glutarate aminotransferase inhibited L-beta-aminoisobutyrate aminotransferase activity in rat liver in the same way as beta-alanine-oxo-glutarate aminotransferase activity. |
last changed |
2009/04/30 10:32 |
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