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Literature summary for 6.1.1.6 extracted from

  • Kisselev, L.L.; Baturina, I.D.
    Two enzymatically active forms of lysyl-tRNA synthetase from E. coli B (1972), FEBS Lett., 22, 231-234.
    View publication on PubMed
Search for more literature for 6.1.1.6

Inhibitors

Inhibitors Comment Organism Structure
KCl
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 tRNALys aminoacylation, enzyme form EI Escherichia coli
0.005
-
 L-Lys
-
 Escherichia coli
0.0057
-
 tRNALys aminoacylation, enzyme form EII Escherichia coli
0.006
-
 L-Lys aminoacylation, enzyme form EI Escherichia coli
0.037
-
 ATP aminoacylation, enzyme form EII Escherichia coli
0.33
-
 ATP aminoacylation, enzyme form EI Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
90000
-
 gel filtration Escherichia coli
100000
-
 sucrose density gradient centrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 B
-
Escherichia coli B / ATCC 11303
-
 B
-

Purification (Commentary)

Purification (Comment) Organism
two enzymatically active forms Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
405
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + lysine + tRNALys
-
 Escherichia coli AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + lysine + tRNALys
-
 Escherichia coli B / ATCC 11303 AMP + L-lysyl-tRNALys + diphosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 5 min, 80% loss of activity Escherichia coli