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  • Title: Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy.
    Author: Storici P, Capitani G, De Biase D, Moser M, John RA, Jansonius JN, Schirmer T.
    Journal: Biochemistry; 1999 Jul 06; 38(27):8628-34. PubMed ID: 10393538.
    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.
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