Aspartate:2-oxoglutarate aminotransferase from Trichomonas vaginalis: comparison with pig heart cytoplasmic enzyme.
The aspartate:2-oxoglutarate aminotransferase from the protozoon Trichomonas vaginalis exists as a mixture of sub-forms of identical Mr and amino acid composition, and of similar catalytic properties. The amino acid composition closely resembles that of aspartate aminotransferase from prokaryotic and vertebrate sources. Some molecular and catalytic properties of the T. vaginalis aspartate aminotransferase are compared with those of the cytoplasmic pig heart enzyme. A major difference is in the ability of the trichomonal enzyme to transaminate aromatic amino acids and 2-oxo acids. A range of inhibitors have been used to compare the active-site regions of the T. vaginalis and cytoplasmic pig heart aspartate aminotransferases.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001219:Aspartate Aminotransferases / Q000302:isolation & purification / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine / Q000378:metabolism*; D014246:Trichomonas vaginalis / Q000201:enzymology*; D014444:Tyrosine Transaminase / Q000378:metabolism
D000596:Amino Acids; D001219:Aspartate Aminotransferases; D014444:Tyrosine Transaminase