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Literature summary extracted from

  • Gasparini, S.; Vincendon, P.; Eriani, G.; Gangloff, J.; Boulanger, Y.; Reinbolt, J.; Kern, D.
    Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae (1991), Biochemistry, 30, 4284-4289.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.12 mutants with substituted His residues expressed in Escherichia coli Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.12 H116G mutants with substituted His residues, His116Gly mutant with a slightly reduced rate of amino acid activation without affecting the other kinetic parameters, His271Gly mutant with completely destroyed activity, His332Gly mutant with 60% decrease in rate of tRNA aminoacylation and no significant changes in the other parameters, His334Gly mutant with 70% decrease in amino acid activation, complete loss of tRNA aspartylation and slightly increased Km for ATP, His271Ala mutant with 25% decrease in the rate of tRNA charging. His334 seems do be part of the active site, while His271 and His332 play an important structural role Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.12 diethyldicarbonate reversed by hydroxylamine Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.12 cytoplasm
-
 Saccharomyces cerevisiae 5737
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Organism

EC Number Organism UniProt Comment Textmining
6.1.1.12 Saccharomyces cerevisiae
-
 mutants with substituted His residues, expressed in Escherichia coli
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.12 ATP + L-aspartate + tRNAAsp
-
 Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
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