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Information on EC 6.1.1.6 - lysine-tRNA ligase and Organism(s) Geobacillus stearothermophilus and UniProt Accession Q9RHV9
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6.1.1.6 lysine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.6
- synthetases
- aminoacylation
- lysylation
-
anticodon
-
aarss
-
isoacceptors
-
diadenosine
- aspartyl-trna
-
gagpol
- tetraphosphate
- trnalys3
- prors
- valrs
- leurs
- arginyl-trna
-
isoleucyl-trna
- glnrs
-
atp-ppi
-
anticodon-binding
-
prolyl-trna
-
multi-trna
- asprs
- diagnostics
- pharmacology
- medicine
- drug development
- synthesis
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysyl-trna synthetase, lysrs, lysrs1, lysrs2, lysyl trna synthetase, mitochondrial lysyl-trna synthetase, cytoplasmic lysyl-trna synthetase, class i lysrs, premsk1p, pfkrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-Lysine-transfer RNA ligase
Lysine translase
Lysine--tRNA ligase
Lysine-tRNA synthetase
LysRS
Lysyl-transfer ribonucleate synthetase
Lysyl-transfer RNA synthetase
Lysyl-tRNA synthetase
Synthetase, lysyl-transfer ribonucleate
L-Lysine-transfer RNA ligase
-
-
-
-
Lysine translase
-
-
-
-
Lysine--tRNA ligase
-
-
-
-
Lysine-tRNA synthetase
-
-
-
-
LysRS
-
-
-
-
Lysyl-transfer ribonucleate synthetase
-
-
-
-
Lysyl-transfer RNA synthetase
-
-
-
-
Lysyl-tRNA synthetase
-
-
-
-
Synthetase, lysyl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
residue Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
sequential ordered mechanism
-
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
Trp314 is involved in binding of L-lysine, binding renders the non-polar microenvironment of the residue more polar
-
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
two-step binding mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9031-26-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the L-lysine binding process is much faster than the ATP binding process
-
r
ATP + L-lysine amide + tRNALys
AMP + L-amino-lysyl-tRNALys + diphosphate
-
-
-
r
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
-
-
r
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
r
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
two-step reaction mechansim, the first step of formation of the aminoacylated enzyme-AMP intermediate is reversible, the second of amino acid transfer to the tRNA is not, binding of L-lysine alone influences the fluorescence of the enzyme, while binding of ATP does not
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
hyperbolic dependence of kapp on the initial ATP concentration, ATP binding to the enzyme-L-lysine complex follows a two-step mechanism
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
substrate inhibition in the aminoacylation reaction above 0.4 mM, no inhibition in the ATP-diphosphate exchange reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
L-lysine
recombinant T7-tagged enzyme, pH 8.0, 30°C
0.038
ATP
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
0.043
ATP
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.049
ATP
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
0.066
ATP
-
aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
0.009
L-lysine
-
ATP-diphosphate exchange reaction, recombinant wild-type enzyme and mutant W314F/W332F, pH 8.0, 37°C
0.01
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C
0.016
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.017
L-lysine
-
aminoacylation reaction, recombinant mutants W314F and W314F/W332F, pH 8.0, 37°C
0.018
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C
0.022
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
8.1
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
hyperbolic dependence of kapp on the initial ATP concentration
-
4.1
L-lysine
recombinant T7-tagged enzyme, pH 8.0, 30°C
0.3
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
34.7
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
36.4
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C
37.3
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
38.6
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C
42.8
ATP
-
ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3 - 6
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.13
L-lysine
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
3.13
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.23
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.3
L-lysine
-
aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
3.53
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.58
L-lysine
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57700
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of two complexes of LysRS with the adenylate of L-lysine hydroxamate and with 5'-O-[N-(L-Lysyl)sulphamoyl] adenosine. The comparisons of the two structures and the SerRS structure reveals the specific side-chain shift of Glu411 of LysRS in the complex with the adenylate of L-lysine hydroxamate. Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAT W314F
mutant of the truncated C-terminal catalytic domain CAT
CAT W332F
mutant of the truncated C-terminal catalytic domain CAT
GsLysRS W314F
mutant of Geobacillus stearothermophilus lysyl-tRNA synthetase
GsLysRS W332F
mutant of Geobacillus stearothermophilus lysyl-tRNA synthetase
W314F
-
site-directed mutagenesis, activity is similar to the wild-type enzyme
W314f/W332F
-
site-directed mutagenesis, slightly reduced activity
W332F
-
site-directed mutagenesis, activity is slightly reduced, but the binding of L-lysine is altered, increased Km for L-lysine
Y271F
-
site-directed mutagenesis, highly increased Km for L-lysine in the ATP-diphosphate exchange reaction
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
after 4 h complete loss of aminoacylation activity, 3 min, stable in presence of all substrates except lysine
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant T7-tagged enzyme from Escherichia coli BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression as T7-tagged enzyme in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Samuelsson, T.; Lundvik, L.
Purification and some properties of asparagine, lysine, serine, and valine:tRNA ligases from Bacillus stearothermophilus
J. Biol. Chem.
253
7033-7039
1978
Geobacillus stearothermophilus
Takita, T.; Ohkubo, Y.; Shima, H.; Muto, T.; Shimizu, N.; Sukata, H.; Ito, Y.; Saito, Y.; Inouye, K.; Hiromi, K.; Tonomura, B.
Lysyl-tRNA synthetase from Bacillus stearothermophilus. Purification and fluorometric and kinetic analysis of the binding of substrates, L-lysine and ATP
J. Biochem.
119
680-689
1996
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA1503
Takita, T.; Shimizu, N.; Sukata, T.; Hashimoto, S.; Akita, E.; Yokota, T.; Esaki, N.; Soda, K.; Inouye, K.; Tonomura, B.i.
Lysyl-tRNA synthetase of Bacillus stearothermophilus:molecular cloning and expression of the gene
Biosci. Biotechnol. Biochem.
64
432-437
2000
Geobacillus stearothermophilus (Q9RHV9), Geobacillus stearothermophilus
Takita, T.; Akita, E.; Inouye, K.; Tonomura, B.i.
Lysyl-tRNA synthetase from Bacillus stearothermophilus. Stopped-flow kinetic analysis of enzyme.lysyladenylate formation
J. Biochem.
124
45-50
1998
Geobacillus stearothermophilus
Takita, T.; Nakagoshi, M.; Inouye, K.; Tonomura, B.i.
Lysyl-tRNA synthetase from Bacillus stearothermophilus: The Trp314 residue is shielded in a non-polar environment and is responsible for the fluorescence changes observed in the amino acid activation reaction
J. Mol. Biol.
325
677-695
2003
Geobacillus stearothermophilus
Saruwatari, Y.; Wada, T.; Takita, T.; Inouye, K.
Substrate-induced conformational changes of the truncated catalytic domain of Geobacillus stearothermophilus lysyl-tRNA synthetase as examined by fluorescence
Biochim. Biophys. Acta
1784
1633-1640
2008
Geobacillus stearothermophilus (Q9RHV9), Geobacillus stearothermophilus
Sakurama, H.; Takita, T.; Mikami, B.; Itoh, T.; Yasukawa, K.; Inouye, K.
Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate
J. Biochem.
145
555-563
2009
Geobacillus stearothermophilus (Q9RHV9), Geobacillus stearothermophilus
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