Probing the active sites of aspartate: 2-oxoglutarate aminotransferases from Trichomonas vaginalis and pig heart cytoplasm using substrate analogues.
1. Series of structural analogues of the substrates and products of the aspartate: 2-oxoglutarate aminotransferase reaction have been tested as reversible inhibitors of the purified aspartate aminotransferases from the protozoon Trichomonas vaginalis and from pig heart cytoplasm. 2. The results highlight differences and similarities between the active site regions of the two enzymes which are relevant to a better understanding of the nature of the enzyme/substrate interactions which influence substrate specificity.
D000596:Amino Acids / Q000494:pharmacology; D000818:Animals; D001219:Aspartate Aminotransferases / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D001667:Binding, Competitive; D003998:Dicarboxylic Acids / Q000494:pharmacology; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine / Q000378:metabolism*; D014246:Trichomonas vaginalis / Q000201:enzymology*
D000596:Amino Acids; D003998:Dicarboxylic Acids; D001219:Aspartate Aminotransferases