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Literature summary for 6.1.1.6 extracted from

  • Jakubowski, H.
    Misacylation of tRNALys with noncognate amino acids by lysyl-tRNA synthetase (1999), Biochemistry, 38, 8088-8093.
    View publication on PubMed
Search for more literature for 6.1.1.6

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol activates 30fold the aminoacylation raection Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in strain JM101 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + lysine + tRNALys Escherichia coli the enzymes major function is to provide Lys-tRNALys fpr protein biosynthesis AMP + L-lysyl-tRNALys + diphosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 homogenously purified recombinant enzyme, class II enzyme
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys two-step reaction mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 editing and aminoacylation reaction with several amino acids, up to 500fold variations in catalytic efficiencies Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + diphosphate + L-arginyl-tRNALys
-
 Escherichia coli ATP + L-arginine + tRNALys
-
 r
AMP + diphosphate + L-lysyl-tRNALys
-
 Escherichia coli ATP + L-lysine + tRNALys
-
 r
AMP + diphosphate + L-methionyl-tRNALys
-
 Escherichia coli ATP + L-methionine + tRNALys
-
 r
AMP + L-threonyl-tRNALys + diphosphate
-
 Escherichia coli ATP + L-threonine + tRNALys
-
 r
ATP + L-alanine + tRNALys 264000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-alanyl-tRNALys + diphosphate
-
 r
ATP + L-arginine + tRNALys best noncognate amino acid substrate, 1600fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-arginyl-tRNALys + diphosphate
-
 r
ATP + L-cysteine + tRNALys 750000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-cysteinyl-tRNALys + diphosphate
-
 r
ATP + L-leucine + tRNALys 132000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-leucyl-tRNALys + diphosphate
-
 r
ATP + L-lysine a small fraction of lysine is converted to lysine lactam in absence or presence of tRNALys Escherichia coli ?
-
 ?
ATP + L-lysine + tRNALys cognate amino acid, best substrate, two-step reaction mechanism, limited selectivity in the aminoacylation reaction due to inefficient editing of some amino acids, e.g. Met, Leu, Cys, Ala, Thr, by pre-transfer mechanism or the absence of post-transfer editing of other amino acids e.g. Arg, Ser, a small fraction of lysine is converted to lysine lactam Escherichia coli AMP + L-lysyl-tRNALys + diphosphate
-
 r
ATP + L-methionine + tRNALys 32000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-methionyl-tRNALys + diphosphate
-
 r
ATP + L-ornithine L-ornithine is converted to ornithine lactam in absence or presence of tRNALys Escherichia coli ?
-
 ?
ATP + L-serine + tRNALys 562000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-seryl-tRNALys + diphosphate
-
 r
ATP + L-threonine + tRNALys 16000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction Escherichia coli AMP + L-threonyl-tRNALys + diphosphate
-
 r
ATP + lysine + tRNALys the enzymes major function is to provide Lys-tRNALys fpr protein biosynthesis Escherichia coli AMP + L-lysyl-tRNALys + diphosphate
-
 r
additional information the enzyme possesses an efficient pre-transfer editing mechanism which prevents misacylation of tRNALys with ornithine, which results in cyclization to ornithine lactam Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
L-Lysine-transfer RNA ligase
-
 Escherichia coli
Lysine translase
-
 Escherichia coli
Lysine--tRNA ligase
-
 Escherichia coli
Lysine-tRNA synthetase
-
 Escherichia coli
LysRS
-
 Escherichia coli
Lysyl-transfer ribonucleate synthetase
-
 Escherichia coli
Lysyl-transfer RNA synthetase
-
 Escherichia coli
Lysyl-tRNA synthetase
-
 Escherichia coli
Synthetase, lysyl-transfer ribonucleate
-
 Escherichia coli

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00023
-
 L-lysyl-tRNALys deacylation reaction, pH 7.4, 37°C, in absence of DTT Escherichia coli
0.00056
-
 L-methionyl-tRNALys deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT Escherichia coli
0.00065
-
 L-lysine L-lysine lactam formation, pH 7.4, 37°C Escherichia coli
0.00067
-
 L-arginyl-tRNALys deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT Escherichia coli
0.00076
-
 L-threonyl-tRNALys deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT Escherichia coli
0.0088
-
 L-lysyl-tRNALys deacylation reaction, pH 7.4, 37°C, in presence of 50 mM DTT Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli