Comparative characterization of Aedes 3‐hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase

FEBS Letters

Han, Qian¹  Li, Jianyong¹ 

[1] Department of Pathobiology, University of Illinois at Urbana-Champaign, 2001 South Lincoln Avenue, Urbana, IL 61802, USA

关键词: 3-Hydroxykynurenine transaminase;    Alanine glyoxylate transaminase;    Serine pyruvate aminotransferase;    Aedes;    Drosophila;    Ae;    Aedes aegypti;    AGT;    alanine glyoxylate transaminase;    Dm;    Drosophila melanogaster;    3-HK;    3-hydroxy-DL-kynurenine;    HKT;    3-hydroxykynurenine transaminase;    HTS;    high-titer viral stock;    KAT;    kynurenine aminotransferase;    MOI;    multiplicity of infection;    PLP;    pyridoxal-5′-phosphate;    Spat;    serine pyruvate aminotransferase;    XA;    xanthurenic acid;   

DOI  :  10.1016/S0014-5793(02)03229-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown