Isolation, characterization, and functional expression of kynurenine aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1).

ABSTRACT: This study describes the molecular and biochemical characterization of kynurenine aminotransferase (KAT) from Aedes aegypti mosquitoes. Through screening an A. aegypti larval cDNA library, a 1695-bp full-length cDNA clone with a 1434-bp open reading frame (ORF) was isolated. Its deduced amino acid sequence consists of 477 amino acid residues with a predicted molecular mass of 53,490 and the amino acid sequence shares 47 and 42% identity with KATs from Homo sapiens and Rattus norvegicus, respectively. This putative A. aegypti KAT (AeKAT) has four potential N-glycosylation sites (Asn-Xxx-Trp/Ser) and a typical mitochondrial leader sequence consisting of 49 amino acids at its NH(2)-terminus with a putative cleavage site between Met-49 and Ser-50. A consensus pyridoxal 5'-phosphate (PLP) bindi

SUBMITTER: Fang J 

PROVIDER: S-EPMC2855842 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature