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Literature summary extracted from

  • Dang, C.V.
    High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation (1982), Biochem. Biophys. Res. Commun., 106, 44-47.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.6 Rattus norvegicus
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.6 liver
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Rattus norvegicus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.6 ATP + lysine + tRNALys
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Rattus norvegicus AMP + L-lysyl-tRNALys + diphosphate
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Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.1.1.6 additional information
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24 S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°C, 37°C and 43°C Rattus norvegicus