Information on EC 6.1.1.6 - lysine-tRNA ligase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
6.1.1.6
-
RECOMMENDED NAME
GeneOntology No.
lysine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
tRNA charging
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-26-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene lysK encoding the LysRS1 isozyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
purified recombinant enzyme expressed in Saccharomyces cerevisiae, wild-type and N-terminally truncated form, the latter prepared by proteolytic cleavage by elastase
-
-
Manually annotated by BRENDA team
MRE600
-
-
Manually annotated by BRENDA team
gene lysS, class II enzyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MS
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-chloroadenosine 5'-triphosphate + lysine + tRNALys
2-chloroadenosine 5'-monophosphate + Lys-tRNALys + diphosphate
show the reaction diagram
-
-
-
-
-
AMP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + ?
show the reaction diagram
-
-
-
-
ATP + 4-aminobutanoate + tRNALys
AMP + 4-aminobutyryl-tRNALys + diphosphate
show the reaction diagram
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P3-triphosphate + ?
show the reaction diagram
-
-
-
-
-
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
show the reaction diagram
ATP + D-lysine + tRNALys
AMP + D-lysyl-tRNALys + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-alanine + tRNALys
AMP + L-alanyl-tRNALys + diphosphate
show the reaction diagram
-
264000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
show the reaction diagram
ATP + L-cysteine + tRNALys
AMP + L-cysteinyl-tRNALys + diphosphate
show the reaction diagram
-
750000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-glutamate + tRNALys
AMP + L-glutamyl-tRNALys + diphosphate
show the reaction diagram
-
low activity
-
?
ATP + L-leucine + tRNALys
AMP + L-leucyl-tRNALys + diphosphate
show the reaction diagram
-
132000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-lysinamide + tRNALys
AMP + L-aminolysyl-tRNALys + diphosphate
show the reaction diagram
-
low activity
-
?
ATP + L-lysine
?
show the reaction diagram
-
a small fraction of lysine is converted to lysine lactam in absence or presence of tRNALys
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysGUU
AMP + L-lysyl-tRNALysGUU + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysUCU
AMP + L-lysyl-tRNALysUCU + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUGU
AMP + L-lysyl-tRNALysUGU + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysUUC
AMP + L-lysyl-tRNALysUUC + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysUUG
AMP + L-lysyl-tRNALysUUG + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
show the reaction diagram
ATP + L-lysine + tRNALysUUUmodified
AMP + L-lysyl-tRNALysUUUmodified + diphosphate
show the reaction diagram
-
anticodon variant tRNA substrate from Escherichia coli, t6 modification of base A37
-
?
ATP + L-lysine + tRNATyrCUA
AMP + L-lysyl-tRNATyrCUA + diphosphate
show the reaction diagram
-
has a weak activity to tRNATyrCUA with L-lysine
-
-
?
ATP + L-lysine amide + tRNALys
AMP + L-amino-lysyl-tRNALys + diphosphate
show the reaction diagram
-
-
-
r
ATP + L-lysine ethyl ester + tRNALys
AMP + ethyl-L-lysyl-tRNALys + diphosphate
show the reaction diagram
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
show the reaction diagram
ATP + L-lysine methyl ester + tRNALys
AMP + methyl-L-lysyl-tRNALys + diphosphate
show the reaction diagram
ATP + L-methionine + tRNALys
AMP + L-methionyl-tRNALys + diphosphate
show the reaction diagram
-
32000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-ornithine
?
show the reaction diagram
-
L-ornithine is converted to ornithine lactam in absence or presence of tRNALys
-
?
ATP + L-serine + tRNALys
AMP + L-seryl-tRNALys + diphosphate
show the reaction diagram
-
562000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-threonine + tRNALys
AMP + L-threonyl-tRNALys + diphosphate
show the reaction diagram
-
16000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + lysine + tRNALys
?
show the reaction diagram
-
primary role is the translation of genetic information into protein structure
-
-
-
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
ATP + lysine + tRNALys,3'-59mer
AMP + L-lysyl-tRNALys, 3'-59mer + diphosphate
show the reaction diagram
-
human tRNALys mutant
-
?
ATP + lysine + tRNALysU35A
AMP + L-lysyl-tRNALysU35A + diphosphate
show the reaction diagram
-
human tRNALys mutant, from in vitro translation, very low activity
-
?
ATP + lysine + tRNALysU35C
AMP + L-lysyl-tRNALysU35C + diphosphate
show the reaction diagram
-
human tRNALys mutant, from in vitro translation, 153fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36A
AMP + L-lysyl-tRNALysU36A + diphosphate
show the reaction diagram
-
human tRNALys mutant, from in vitro translation, 182fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36C
AMP + L-lysyl-tRNALysU36C + diphosphate
show the reaction diagram
-
human tRNALys mutant, from in vitro translation, 11fold decreased activity compared to the wild-type
-
?
ATP + ornithine + tRNALys
AMP + ornithyl-tRNALys + diphosphate
show the reaction diagram
dATP + lysine + tRNALys
dAMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
-
-
-
-
-
formycin 5'-triphosphate + L-lysine + tRNALys
formycin 5'-monophosphate + diphosphate + L-lysyl-tRNALys
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
ATP + lysine + tRNALys
?
show the reaction diagram
-
primary role is the translation of genetic information into protein structure
-
-
-
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NH4+
-
synthesis of lysyl-tRNA from lysyl-AMP-enzyme is dependent on NH4+ or other monovalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R,5S)-1-[(6-amino-9H-purin-9-yl)acetyl]-5-carbamoylpyrrolidin-3-yl L-lysylsulfamate
strong inhibitory effect
(4R)-1-[(3-chloro-4-hydroxyphenyl)acetyl]-4-[(L-lysylsulfamoyl)oxy]-L-prolinamide
strong inhibitory effect
(4S)-1-(3-bromo-4-hydroxybenzyl)-4-[hydroxy(L-lysyl)amino]-L-prolinamide
strong inhibitory effect
2'-deoxyadenosine 5'-triphosphate
-
-
2'-O-Methyladenosine 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
3'-O-Methyladenosine 5'-triphosphate
-
-
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
5'-Triphosphates of purine riboside
-
-
6-amino-n-hexanoic acid
-
ATP-diphosphate exchange reaction
8-azidoadenosine
-
-
8-Bromoadenosine
-
-
AEC
-
competitive versus L-lysine
Arabinofuranosyladenosine 5'-triphosphate
-
-
ATP
-
substrate inhibition in the aminoacylation reaction above 0.4 mM, no inhibition in the ATP-diphosphate exchange reaction
cadaverine
cladosporin
-
30% inhibition at 0.11 mM
CNBr
-
treatment of tRNALys substrate with CNBr reduces the enzyme activity
D-Lysine
gamma-aminobutyric acid
-
-
human tRNALys anticodon domain
-
from wild-type tRNALys, N-terminally truncated mutant enzyme
-
human tRNALys,3'-14mer mutant
-
-
-
human tRNALys,3'-17mer mutant
-
-
-
human tRNALys,3'-7mer mutant
-
-
-
human tRNALys-3'oxidized
-
3'-oxidized by periodate, N-terminally truncated mutant enzyme
-
human tRNALysU35G anticodon domain
-
N-terminally truncated mutant enzyme
-
human tRNALysU35G mutant
-
defective substrate in both binding and catalysis, N-terminally truncated mutant enzyme
-
L-Lysine amide
L-Lysine ethyl ester
-
-
L-Lysine hydrazide
-
-
L-Lysine hydroxamate
-
ATP-diphosphate exchange reaction
L-Lysine methyl ester
-
-
lysinamide
-
competitive versus L-lysine
lysine ethyl ester
-
competitive versus L-lysine
lysine methyl ester
-
competitive versus L-lysine
Mg2+
-
synthesis of lysyl-tRNA from lysyl-AMP-enzyme inhibited, formation of Lys-tRNALys from lysine, tRNA and ATP-enzyme complex or ATP is dependent on Mg2+
Nepsilon-Acetyl-L-lysine
-
ATP-diphosphate exchange reaction
NH4+
-
formation of Lys-tRNALys from lysine, tRNA and ATP-enzyme complex or ATP
ornithine
-
competitive versus L-lysine
S-(2-aminoethyl)-L-cysteine
tubercidin 5'-triphosphate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
-
stimulation of diadenosine 5',5'''-P1,P4-tetraphosphate synthetase activity
aspartyl-tRNA synthetase
-
EC 6.1.1.12, AspRS, from the multi-synthetase complex. HKRS and hKRSDELTA60 are differentially stimulated by
-
Diphosphatase
-
dithiothreitol
-
activates 30fold the aminoacylation raection
syntenin-1
-
tandem PDZ protein, regulates KRS activity, adaptor modulating the activity of KRS. A point mutation in the PDZ2 domain of syntenin-1 abrogates interaction with KRS
-
translation elongation factor 1alpha
-
EF1alpha, hKRSDELTA60 binds to EF1alpha and is stimulated by EF1alpha in vitro
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
2-Chloroadenosine 5'-triphosphate
-
aminoacylation
1.5
AMP
-
5',5'''-P1,P4-tetraphosphate formation
0.00015 - 9.5
ATP
0.002 - 0.0043
Borellia burgdorferi tRNALys
-
0.0039 - 0.0063
Escherichia coli G2.U71 tRNA
-
0.0015 - 0.0019
Escherichia coli wild-type tRNA
-
0.2
Formycin 5'-triphosphate
-
aminoacylation
0.003 - 0.0117
human tRNALys,3
-
0.0025 - 0.0236
L-Lys
0.0013 - 8.1
L-lysine
0.0024 - 0.0047
Lys
0.000007 - 0.0057
tRNALys
0.00057
tRNALys from rat liver
-
-
-
0.00056 - 1.4
tRNALysCUU
-
0.00033 - 1.5
tRNALysGUU
-
0.0078
tRNALysU35C
-
human mutant tRNALys, 30°C
-
0.0095
tRNALysU36A
-
human mutant tRNALys, 30°C
-
0.0037
tRNALysU36C
-
human mutant tRNALys, 30°C
-
0.0018
tRNALysUGU
-
-
-
0.0028
tRNALysUUC
-
-
-
0.0004 - 5.1
tRNALysUUU
-
0.0015
tRNALysUUUmodified
-
-
-
0.00145
tRNATyrCUA
-
-
-
0.002 - 0.0028
yeast tRNALys
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2
aminoacylation
Geobacillus stearothermophilus
-
-
-
0.00067
Arg-tRNALys
Escherichia coli
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.00051 - 42.8
ATP
0.0035 - 6.08
Borellia burgdorferi tRNALys
-
0.0025 - 0.0035
Escherichia coli G2.U71 tRNA
-
0.004
Escherichia coli tRNALys
Methanococcus maripaludis
-
recombinant enzyme, pH 7.2, 37°C
-
0.002
Escherichia coli tRNALys CNBr-treated
Methanococcus maripaludis
-
recombinant enzyme, pH 7.2, 37°C
-
0.004 - 0.055
Escherichia coli wild-type tRNA
-
6.2 - 7.8
human tRNALys,3
-
0.00012 - 85
L-lysine
14.5
L-Lysine amide
Geobacillus stearothermophilus
-
forward reaction, pH 8.0, 30°C
221
L-Lysine hydroxamate
Geobacillus stearothermophilus
-
forward reaction, pH 8.0, 30°C
0.00023 - 0.0088
Lys-tRNALys
2.7 - 5.5
lysylation
-
0.00056
Met-tRNALys
Escherichia coli
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
0.2
Methanococcus maripaludis tRNALys
Methanococcus maripaludis
-
recombinant enzyme, pH 7.2, 37°C
-
0.05
Methanococcus maripaludis tRNALys CNBr-treated
Methanococcus maripaludis
-
recombinant enzyme, pH 7.2, 37°C
-
0.00076
Thr-tRNALys
Escherichia coli
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.34 - 2
tRNALys
0.00026 - 6.08
tRNALys,3'-59mer
-
0.014 - 0.062
tRNALysCUU
-
0.0095 - 0.043
tRNALysGUU
-
0.0079
tRNALysU35C
Homo sapiens
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.0068
tRNALysU36A
Homo sapiens
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.046
tRNALysU36C
Homo sapiens
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.0004
tRNALysUGU
Borreliella burgdorferi
-
-
-
0.00018
tRNALysUUC
Borreliella burgdorferi
-
-
-
0.00012 - 0.68
tRNALysUUU
-
0.12
tRNALysUUUmodified
Borreliella burgdorferi
-
-
-
0.013
tRNATyrCUA
Escherichia coli
-
-
-
6.3 - 7.1
yeast tRNALys
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 400
L-lysine
134
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02761
(3R,5S)-1-[(6-amino-9H-purin-9-yl)acetyl]-5-carbamoylpyrrolidin-3-yl L-lysylsulfamate
-
0.03442
(4R)-1-[(3-chloro-4-hydroxyphenyl)acetyl]-4-[(L-lysylsulfamoyl)oxy]-L-prolinamide
-
0.00995
(4S)-1-(3-bromo-4-hydroxybenzyl)-4-[hydroxy(L-lysyl)amino]-L-prolinamide
-
0.00001 - 0.0013
5'-O-[N-(L-lysyl)sulfamoyl]adenosine
12
D-Lysine
-
pH 7.2, 37°C
0.005
human tRNALys anticodon domain
-
30°C, N-terminally truncated mutant enzyme
-
0.0013
human tRNALys-3'oxidized
-
3'-oxidized by periodate, 30°C, N-terminally truncated mutant enzyme
-
0.005
human tRNALysU35G anticodon domain
-
30°C, N-terminally truncated mutant enzyme
-
0.042
human tRNALysU35G mutant
-
30°C, N-terminally truncated mutant enzyme
-
5
L-arginine
-
pH 7.2, 37°C
0.0015 - 19
S-(2-aminoethyl)-L-cysteine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000454 - 0.0000896
cladosporin
0.015
Zn2+
Escherichia coli
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00002
purified recombinant isozyme, mitochondrial tRNALys substrate
0.0001
purified recombinant isozyme, mitochondrial tRNALys substrate
0.0032
purified recombinant isozyme, cytoplasmic tRNALys substrate
0.0133
purified recombinant isozyme, cytoplasmic tRNALys substrate
19.6
-
ATP-diphosphate exchange
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
50
-
aminoacylation reaction and ATP-diphosphate exchange, pH 8
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
inactive at 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
-
recombinant N-terminal extension, calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
HIV-1 producing
Manually annotated by BRENDA team
-
cell line LCC-RK1
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts
Manually annotated by BRENDA team
-
KARS also occurs in the supernatant of stressed cells
-
Manually annotated by BRENDA team
-
associated with
-
Manually annotated by BRENDA team
-
associated with
Manually annotated by BRENDA team
additional information
-
anthracyclin-induced translocation of KARS from the endoplasmic reticulum to the cell surface
-
Manually annotated by BRENDA team