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
Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy / Storici, P; Capitani, G; DE BIASE, Daniela; Moser, M; John, Ra; Jansonius, Jn; Schirmer, T.. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 38:(1999), pp. 8628-8634. [10.1021/bi990478j]
Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy.
DE BIASE, Daniela;
1999
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 siteI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
