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Literature summary for 6.1.1.9 extracted from

  • Bee, G.; Waller, J.P.
    Valyl-tRNA synthetase from rabbit liver. II. The enzyme derived from the high-Mr complex displays hydrophobic as well as polyanion-binding properties (1989), J. Biol. Chem., 264, 21138-21143.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
1 * 125000, SDS-PAGE Saccharomyces cerevisiae
135000
-
glycerol density gradient centrifugation Oryctolagus cuniculus
140000
-
1 * 140000, SDS-PAGE Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae D273
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-

Storage Stability

Storage Stability Organism
-20°C, 50% glycerol, 0.1% detergent, stable for several months Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-valine + tRNAVal
-
Saccharomyces cerevisiae AMP + diphosphate + L-valyl-tRNAVal
-
?
ATP + L-valine + tRNAVal
-
Oryctolagus cuniculus AMP + diphosphate + L-valyl-tRNAVal
-
?
ATP + L-valine + tRNAVal
-
Saccharomyces cerevisiae D273 AMP + diphosphate + L-valyl-tRNAVal
-
?

Subunits

Subunits Comment Organism
?
-
Oryctolagus cuniculus
monomer 1 * 140000, SDS-PAGE Oryctolagus cuniculus
monomer 1 * 125000, SDS-PAGE Saccharomyces cerevisiae