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Literature summary for 6.1.1.6 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
Search for more literature for 6.1.1.6

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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)

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

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LysRS
-
 Bacillus cereus
Lysyl-tRNA synthetase
-
 Bacillus cereus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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
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

Cofactor Comment Organism Structure
ATP
-
 Bacillus cereus

kcat/KM [mM/s]

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