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Literature summary for 6.1.1.17 extracted from

  • Thomes, J.C.; Ratinaud, M.H.; Julien, R.
    Dimeric glutamyl-tRNA synthetases from wheat. Kinetic properties and functional structures (1983), Eur. J. Biochem., 135, 479-484.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0002
-
tRNAGlu enzyme forms GluRSC and GluRSP, aminoacylation Triticum aestivum
0.00044
-
tRNAGlu enzyme form GluRSE, aminoacylation Triticum aestivum
0.01
-
Glu enzyme form GluRSC, aminoacylation Triticum aestivum
0.083
-
Glu enzyme forms GluRSP and GluRSE, aminoacylation Triticum aestivum

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast enzyme form GluRSC Triticum aestivum 9507
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Triticum aestivum
Mg2+ Km: 0.46 mM, enzyme form GluRSC, aminoacylation, Km: 0.38 mM, enzyme form GluRSP, aminoacylation Triticum aestivum
Mg2+ Km: 0.28 mM, enzyme form GluRSE, aminoacylation Triticum aestivum

Organism

Organism UniProt Comment Textmining
Triticum aestivum
-
enzyme forms: GuRSP and GluRSE
-

Source Tissue

Source Tissue Comment Organism Textmining
germ 2 enzyme forms: GluRSP and GluRSE Triticum aestivum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
Triticum aestivum AMP + diphosphate + L-glutamyl-tRNAGlu
-
?

Subunits

Subunits Comment Organism
dimer the active forms are dimers, which are in equilibrium with inactive monomers Triticum aestivum