title: Nucleotide sequence and deduced amino acid sequence of a putative asparagine synthetase in the mosquito Aedes aegypti (L.).
abstract: 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.
authors.affiliation: Zoologisches Institut, Universität Zürich-Irchel, Switzerland.
authors.forename: U
authors.initials: U
authors.lastname: Ackermann
authors.forename: R
authors.initials: R
authors.lastname: Graf
mesh_terms: D000330:Aedes / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001217:Aspartate-Ammonia Ligase / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D008969:Molecular Sequence Data
chemical_list: D018076:DNA, Complementary; D001217:Aspartate-Ammonia Ligase