Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Han Q,Li Jdoi
10.1016/s0014-5793(02)03229-5keywords:
subject
Has Abstractpub_date
2002-09-11 00:00:00pages
199-204issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302032295journal_volume
527pub_type
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