ArticleThe Biochemical journal2006
Evolution of two alanine glyoxylate aminotransferases in mosquito.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Unraveling forensic timelines using molecular markers in Phormia regina maggots.PLoS genetics · 2025Article
- Inhibition of 3-Hydroxykynurenine Transaminase fromACS bio & med chem Au · 2023Article
- Biochemical Evolution of a Potent Target of Mosquito Larvicide, 3-Hydroxykynurenine Transaminase.Molecules (Basel, Switzerland) · 2022Article
- A second generation of 1,2,4-oxadiazole derivatives with enhanced solubility for inhibition of 3-hydroxykynurenine transaminase (HKT) fromRSC medicinal chemistry · 2021Article
- Genome and transcriptome analyses provide insight into the euryhaline adaptation mechanism of Crassostrea gigas.PloS one · 2013Article
- Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.The Biochemical journal · 2012Article
- The tryptophan oxidation pathway in mosquitoes with emphasis on xanthurenic acid biosynthesis.Journal of insect physiology · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In the mosquito, transamination of 3-HK (3-hydroxykynurenine) to XA (xanthurenic acid) is catalysed by an AGT (alanine glyoxylate aminotransferase) and is the major branch pathway of tryptophan metabolism. Interestingly, malaria parasites hijack this pathway to use XA as a chemical signal for development in the mosquito. Here, we report that the mosquito has two AGT isoenzymes. One is the previously cloned AeHKT [Aedes aegypti HKT (3-HK transaminase)] [Han, Fang and Li (2002) J. Biol. Chem. 277, 15781-15787], similar to hAGT (human AGT), which primarily catalyses 3-HK to XA in mosquitoes, and the other is a typical dipteran insect AGT. We cloned the second AGT from Ae. aegypti mosquitoes [AeAGT (Ae. aegypti AGT)], overexpressed the enzyme in baculovirus/insect cells and determined its biochemical characteristics. We also expressed hAGT for a comparative study. The new cloned AeAGT is highly substrate-specific when compared with hAGT and the previously reported AeHKT and Drosophila AGT, and is translated mainly in pupae and adults, which contrasts with AeHKT that is expressed primarily in larvae. Our results suggest that the physiological requirements of mosquitoes and the interaction between the mosquito and its host appear to be the driving force in mosquito AGT evolution.
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