|
type |
Journal Article |
authors |
Han, Q.; Li, J. |
title |
Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase |
journal |
FEBS Lett |
Activity |
2.6.1.44 |
Family |
2.6.1.44.a |
sel |
selected |
ui |
12220660 |
year |
(2002) |
volume |
527 |
number |
1-3 |
pages |
199-204 |
| |
abstract |
This study describes the comparative analysis of two insect recombinant aminotransferases, Aedes aegypti 3-hydroxykynurenine (3-HK) transaminase/alanine glyoxylate aminotransferase (Ae-HKT/AGT) and Drosophila melanogaster serine pyruvate aminotransferase (Dm-Spat), which share 52% identity in their amino acid sequences. Both enzymes showed AGT activity. In addition, Ae-HKT/AGT is also able to catalyze the transamination of 3-HK or kynurenine with glyoxylate, pyruvate or oxaloacetate as the amino acceptor. Kinetic analysis and other data suggest that Ae-HKT/AGT plays a critical role in mosquito tryptophan catabolism by detoxifying 3-HK and that Dm-Spat is primarily involved in glyoxylate detoxification. |
last changed |
2019/08/19 10:01 |
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