Nucleotide sequence and deduced amino acid sequence of a putative asparagine synthetase in the mosquito Aedes aegypti (L.).

Autor(es): Ackermann U; Graf R

Resumo: A cDNA was cloned from a Aedes aegypti head cDNA library, containing the complete coding sequence for an asparagine synthetase homolog. The predicted polypeptide sequence exhibits high homology with different proteins of the 'purF' glutamine amidotransferase enzyme family. The aminoterminal region, containing Cys-1 which is crucial to perform the glutaminase reaction, was highly conserved among the asparagine synthetase family. Subsequent expression of the cDNA yielded a 54,000 Da protein corresponding to the molecular weight of other asparagine synthetases.

Palavras-Chave: `purF' glutamine amidotransferase; Glutaminase activity; Asparagine synthesis; cDNA sequence; cDNA expression; Baculovirus expression system

Imprenta: Biochimica et Biophysica Acta, v. 1383, n. 2, p. 179-182, 1998

Identificador do objeto digital: 10.1016/S0167-4838(98)00008-9

Descritores: Aedes aegypti - DNA ; Aedes aegypti - Molecular Structure ; Aedes aegypti - Pathogenesis ; Aedes aegypti - Proteins

Data de publicação: 1998