|
type |
Journal Article |
authors |
Storici, P.; Capitani, G.; De Biase, D.; Moser, M.; John, R. A.; Jansonius, J. N.; Schirmer, T. |
title |
Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy |
journal |
Biochemistry |
Activity |
2.6.1.19 |
Family |
2.6.1.19.a |
sel |
selected |
ui |
10393538 |
year |
(1999) |
volume |
38 |
number |
27 |
pages |
8628-34 |
| |
keywords |
4-Aminobutyrate Transaminase/*chemistry |
abstract |
gamma-Aminobutyrate aminotransferase (GABA-AT), a pyridoxal phosphate- dependent enzyme, is responsible for the degradation of the inhibitory neurotransmitter GABA and is a target for antiepileptic drugs because its selective inhibition raises GABA concentrations in brain. The X-ray structure of pig GABA-AT has been determined to 3.0 A resolution by molecular replacement with the distantly related enzyme ornithine aminotransferase. Both omega-aminotransferases have the same fold, but exhibit side chain replacements in the closely packed binding site that explain their respective specificities. The aldimines of GABA and the antiepileptic drug vinyl-GABA have been modeled into the active site. |
last changed |
2009/06/30 19:27 |
|