Literature summary for 6.1.1.12 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.

Search for more literature for 6.1.1.12

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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

Inhibitors	Comment	Organism	Structure
diethyldicarbonate	reversed by hydroxylamine	Saccharomyces cerevisiae

Localization

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

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	mutants with substituted His residues, expressed in Escherichia coli	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)