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

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 Lett

journal_title

FEBS letters

authors

Han Q,Li J

doi

10.1016/s0014-5793(02)03229-5

keywords:

subject

Has Abstract

pub_date

2002-09-11 00:00:00

pages

199-204

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302032295

journal_volume

527

pub_type

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