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Literature summary for 6.1.1.6 extracted from

  • Wahab, S.Z.; Yang, D.C.H.
    Comparison of the enzymatic behavior of high molecular weight and free lysyl-tRNA synthetase from rat liver. Kinetic analysis of lysylation of tRNA (1986), Arch. Biochem. Biophys., 249, 407-417.
    View publication on PubMed
Search for more literature for 6.1.1.6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000007
-
 tRNALys lysylation, free enzyme Rattus norvegicus
0.00002
-
 tRNALys lysylation, 18S synthetase complex Rattus norvegicus
0.0037
-
 Lys lysylation, 18S synthetase complex Rattus norvegicus
0.0047
-
 Lys lysylation, free enzyme Rattus norvegicus
0.005
-
 L-Lys ATP, , lysylation, free enzyme Rattus norvegicus
0.01
-
 ATP lysylation, 28S synthetase complex Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-lysine + tRNALys
-
 Rattus norvegicus AMP + diphosphate + L-lysyl-tRNALys
-
 r
ATP + lysine + tRNALys
-
 Rattus norvegicus AMP + L-lysyl-tRNALys + diphosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7
-
 tRNALys 18S synthetase complex Rattus norvegicus
5.5
-
 tRNALys free enzyme Rattus norvegicus