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Literature summary for 6.1.1.6 extracted from

  • Levengood, J.D.; Ataide, S.F.; Roy, H.; Ibba, M.
    Divergence in non-cognate amino acid recognition between class I and class II lysyl-tRNA synthetases (2004), J. Biol. Chem., 279, 17707-17714.
    View publication on PubMed
Search for more literature for 6.1.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in strain BL21(DE3) Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
 Borreliella burgdorferi
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
-
 Escherichia coli
AEC competitive versus L-lysine Escherichia coli
cadaverine
-
 Escherichia coli
D-Lysine competitive versus L-lysine Escherichia coli
gamma-aminobutyric acid
-
 Borreliella burgdorferi
L-arginine
-
 Borreliella burgdorferi
lysinamide competitive versus L-lysine Escherichia coli
lysine ethyl ester competitive versus L-lysine Escherichia coli
lysine methyl ester competitive versus L-lysine Escherichia coli
additional information no inhibition by lysinamide in vivo Borreliella burgdorferi
ornithine competitive versus L-lysine Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-lysine + tRNALys Escherichia coli
-
 AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine + tRNALys Borreliella burgdorferi
-
 AMP + L-lysyl-tRNALys + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Borreliella burgdorferi
-
 purified enzyme from Bacillus subtilis strain 157.1, class I enzyme
-
Escherichia coli
-
 gene lysS, class II enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from strain BL21(DE3) Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys active site structure Escherichia coli
a
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys active site structure Borreliella burgdorferi
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 4-aminobutanoate + tRNALys
-
 Escherichia coli AMP + 4-aminobutyryl-tRNALys + diphosphate
-
 ?
ATP + D-lysine + tRNALys
-
 Escherichia coli AMP + D-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-arginine + tRNALys low activity Escherichia coli AMP + L-arginyl-tRNALys + diphosphate
-
 ?
ATP + L-glutamate + tRNALys low activity Escherichia coli AMP + L-glutamyl-tRNALys + diphosphate
-
 ?
ATP + L-lysinamide + tRNALys low activity Escherichia coli AMP + L-aminolysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine + tRNALys
-
 Escherichia coli AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine + tRNALys
-
 Borreliella burgdorferi AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine + tRNALys 2-step reaction, the first step comprises the activation of the amino acid to form an enzyme-bound aminoacyl adenylate, the second step involves binding of this complex by tRNA, whose 3'-end is esterified with the aminoacyl-moiety followed by release of the resulting aminoacyl-tRNA, aminoacylation can be performed in absence of the tRNA Escherichia coli AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine + tRNALys 2-step reaction, the first step comprises the activation of the amino acid to form an enzyme-bound aminoacyl adenylate, the second step involves binding of this complex by tRNA, whose 3'-end is esterified with the aminoacyl-moiety followed by release of the resulting aminoacyl-tRNA, aminoacylation cannot be performed in absence of the tRNA Borreliella burgdorferi AMP + L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine ethyl ester + tRNALys
-
 Escherichia coli AMP + ethyl-L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine ethyl ester + tRNALys
-
 Borreliella burgdorferi AMP + ethyl-L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine hydroxamate + tRNALys
-
 Escherichia coli AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine methyl ester + tRNALys
-
 Escherichia coli AMP + methyl-L-lysyl-tRNALys + diphosphate
-
 ?
ATP + L-lysine methyl ester + tRNALys
-
 Borreliella burgdorferi AMP + methyl-L-lysyl-tRNALys + diphosphate
-
 ?
ATP + ornithine + tRNALys
-
 Escherichia coli AMP + ornithyl-tRNALys + diphosphate
-
 ?
ATP + ornithine + tRNALys low activity Borreliella burgdorferi AMP + ornithyl-tRNALys + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
L-Lysine-transfer RNA ligase
-
 Escherichia coli
L-Lysine-transfer RNA ligase
-
 Borreliella burgdorferi
Lysine translase
-
 Escherichia coli
Lysine translase
-
 Borreliella burgdorferi
Lysine--tRNA ligase
-
 Escherichia coli
Lysine--tRNA ligase
-
 Borreliella burgdorferi
Lysine-tRNA synthetase
-
 Escherichia coli
Lysine-tRNA synthetase
-
 Borreliella burgdorferi
LysRS
-
 Escherichia coli
LysRS
-
 Borreliella burgdorferi
LysRS1 class I enzyme Borreliella burgdorferi
LysRS2 class II enzyme Escherichia coli
Lysyl-transfer ribonucleate synthetase
-
 Escherichia coli
Lysyl-transfer ribonucleate synthetase
-
 Borreliella burgdorferi
Lysyl-transfer RNA synthetase
-
 Escherichia coli
Lysyl-transfer RNA synthetase
-
 Borreliella burgdorferi
Lysyl-tRNA synthetase
-
 Escherichia coli
Lysyl-tRNA synthetase
-
 Borreliella burgdorferi
Synthetase, lysyl-transfer ribonucleate
-
 Escherichia coli
Synthetase, lysyl-transfer ribonucleate
-
 Borreliella burgdorferi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli
ATP
-
 Borreliella burgdorferi

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5
-
 L-arginine pH 7.2, 37°C Borreliella burgdorferi
12
-
 D-Lysine pH 7.2, 37°C Escherichia coli