Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase.
This study describes the comparative analysis of two insect recombinant aminotransferases, Aedes aegypti 3-hydroxykynurenine (3-HK) transaminase/alanine glyoxylate aminotransferase (Ae-HKT/AGT) and Drosophila melanogaster serine pyruvate aminotransferase (Dm-Spat), which share 52% identity in their amino acid sequences. Both enzymes showed AGT activity. In addition, Ae-HKT/AGT is also able to catalyze the transamination of 3-HK or kynurenine with glyoxylate, pyruvate or oxaloacetate as the amino acceptor. Kinetic analysis and other data suggest that Ae-HKT/AGT plays a critical role in mosquito tryptophan catabolism by detoxifying 3-HK and that Dm-Spat is primarily involved in glyoxylate detoxification.
Han
Qian
Q
Department of Pathobiology, University of Illinois at Urbana-Champaign, 2001 South Lincoln Avenue, Urbana, IL 61802, USA.
Li
Jianyong
J
D000330:Aedes / Q000201:enzymology*; D000818:Animals; D029721:Drosophila Proteins / Q000378:metabolism; D004331:Drosophila melanogaster / Q000201:enzymology*; D006038:Glyoxylates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009097:Multienzyme Complexes / Q000378:metabolism; D062907:Oxaloacetic Acid / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature; D000637:Transaminases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
C467056:3-hydroxykynurenine transaminase-alanine glyoxylate transaminase, Aedes aegypti; D029721:Drosophila Proteins; D006038:Glyoxylates; D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D062907:Oxaloacetic Acid; D000637:Transaminases; C022638:serine-pyruvate aminotransferase; C021481:kynurenine-oxoglutarate transaminase; C031150:glyoxylic acid