Autor(es): Han, Q; Hanyong, LY

Resumo: 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Palavras-Chave: 3-hydroxykynurenine transaminase; Alanine glyoxylate transaminase; Serine pyruvate aminotransferase; Aedes; Drosophila

Imprenta: FEBS Letters, v. 527, n. 1-3, p. 199-204, 2002

Identificador do objeto digital: 10.1016/S0014-5793(02)03229-5

Descritores: Aedes aegypti - Proteins

Data de publicação: 2002

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