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B6db references: 10393538

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
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

B6db references