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Literature summary extracted from

  • Gilreath, M.S.; Roy, H.; Bullwinkle, T.J.; Katz, A.; Navarre, W.W.; Ibba, M.
    Beta-lysine discrimination by lysyl-tRNA synthetase (2011), FEBS Lett., 585, 3284-3288.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.6 expressed in Escherichia coli XL1-Blue cells Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.6 A233S the mutant recognizes L-lysine better than wild type and shows higher catalytic efficiency Bacillus cereus
6.1.1.6 A233S/G469A inactive, the mutation decreases stable L-lysyl-adenylate formation Bacillus cereus
6.1.1.6 G469A very low activity, the mutation decreases stable L-lysyl-adenylate formation Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.6 0.16
-
 L-lysine wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 0.2 1 L-lysine mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 3.9
-
 L-lysine mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.6 ATP + L-lysine + tRNALys Bacillus cereus
-
 AMP + diphosphate + L-lysyl-tRNALys
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.6 Bacillus cereus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.6 TALON metal affinity resin column chromatography Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.6 ATP + L-lysine + tRNALys
-
 Bacillus cereus AMP + diphosphate + L-lysyl-tRNALys
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.6 LysRS
-
 Bacillus cereus
6.1.1.6 Lysyl-tRNA synthetase
-
 Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.6 8.2
-
 L-lysine mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 41.7
-
 L-lysine wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 85
-
 L-lysine mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.6 ATP
-
 Bacillus cereus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.1.1.6 2.2
-
 L-lysine mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 260
-
 L-lysine wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus
6.1.1.6 400
-
 L-lysine mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C Bacillus cereus