Literature summary for 6.1.1.12 extracted from

Eriani, G.; Prevost, G.; Kern, D.; Vincendon, P.; Dirheimer, G.; Gangloff, J.
Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organisation by deletion analysis (1991), Eur. J. Biochem., 200, 337-343.

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Protein Variants

Protein Variants	Comment	Organism
additional information	C-terminal and N-terminal truncated forms. On the C-terminal side, very limited modifications readily affect the enzyme properties. The N-terminal sequence up to amino acid 70 is dispensable for activity, domains beyond amino acid 70 have increasing catalytic importance	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.04	-	ATP	wild-type enzyme	Saccharomyces cerevisiae
0.4	-	Asp	wild-type	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	wild-type, C-terminal, and N-terminal truncated forms	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type and mutant enzymes	Saccharomyces cerevisiae

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)