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Literature summary for 6.1.1.12 extracted from

  • Eriani, G.; Caravelli.J.; Martin, F.; Dirheimer, G.; Moras, D.
    Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline (1993), Proc. Natl. Acad. Sci. USA, 90, 10816-10820.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.12

Crystallization (Commentary)

Crystallization (Comment) Organism
binary complex formed by the enzyme and tRNAAsp Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
P273G Pro273Gly mutant. Catalytic properties of native and Pro273Gly homodimers or heterodimers of AspRS molecules, confirm the participation of Pro273 in subunit association Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km values of ATP-diphosphate exchange reaction and acylation of homodimers and heterodimers of AspRS molecules Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 native and Pro273Gly mutant
-

Substrates and Products (Substrate)

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