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6.1.1.6: lysine-tRNA ligase

This is an abbreviated version!
For detailed information about lysine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.6

Reaction

ATP
+
L-lysine
 +
tRNALys
=
AMP
 +
diphosphate
 +
L-lysyl-tRNALys

Synonyms

Ap4A synthase, BBA_03037, class 1 lysyl tRNA synthetase, class I LysRS, class I lysyl-tRNA synthetase, class II lysyl-tRNA synthetase, cyto-LysRS, cytoKARS, cytoplasmic lysyl-tRNA synthetase, FOSTERSO_4045, GsLysRS, hKRS, KARS, KRS, KRS-1, L-Lysine-transfer RNA ligase, lysine aminoacyl-tRNA synthetase, Lysine translase, Lysine--tRNA ligase, Lysine-tRNA synthetase, LysRS, LysRS-I, LysRS-II, LysRS1, LysRS2, lysS, lysS2, LysU, LysX, lysyl tRNA synthetase, Lysyl-transfer ribonucleate synthetase, Lysyl-transfer RNA synthetase, Lysyl-tRNA synthetase, lysylphosphatidylglycerol biosynthesis bifunctional protein, mito-LysRS, mitochondrial lysyl-tRNA synthetase, mitoKARS, More, Msk1p, MSMEG_3796, MSMEG_6094, MSMEI_3707, MXAN_4731, PF3D7_1350100, PfKRS, preMsk1p, Synthetase, lysyl-transfer ribonucleate, tRK1

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.6 lysine-tRNA ligase

Engineering

Engineering on EC 6.1.1.6 - lysine-tRNA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A233S
-
the mutant recognizes L-lysine better than wild type and shows higher catalytic efficiency
A233S/G469A
-
inactive, the mutation decreases stable L-lysyl-adenylate formation
G469A
-
very low activity, the mutation decreases stable L-lysyl-adenylate formation
E43I
-
significant decrease of catalytic activity compared to the wild type enzyme
E43Q
-
significant decrease of catalytic activity compared to the wild type enzyme
G29A
-
significant decrease of catalytic activity compared to the wild type enzyme
H242A
-
significant decrease of catalytic activity compared to the wild type enzyme
H242L
-
shows almost no change in the catalytic activity compared to the wild type enzyme
H242W
-
significant decrease of catalytic activity compared to the wild type enzyme
T31G
-
significant decrease of catalytic activity compared to the wild type enzyme
T31S
-
shows almost no change in the catalytic activity compared to the wild type enzyme
W220A
-
significant decrease of catalytic activity compared to the wild type enzyme
W220L
-
significant decrease of catalytic activity compared to the wild type enzyme
W220Y
-
significant decrease of catalytic activity compared to the wild type enzyme
Y269F
-
6fold drop in the catalytic efficiency compared to the wild type enzyme
Y269S
-
significant decrease of catalytic activity compared to the wild type enzyme
E240D
-
1.2fold increase in Km-value for Lys, 21fold decrease in turnover number for Lys, Km-value for ATP is nearly identical to wild-type value, 24fold decrease in turnover number for ATP
E240Q
-
1.4fold increase in Km-value for Lys, 207fold decrease in turnover number for Lys, 1.2fold increase in Km-value for ATP, 261fold decrease in turnover number for ATP
E246D
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E246R
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E264A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E264K
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264N
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264Q
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E273A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E278D
-
98fold increase in Km-value for Lys, 11fold decrease in turnover number for Lys, 1.3fold increase in Km-value for ATP, 63fold decrease in turnover number for ATP
E278Q
-
1.9fold decrease in Km-value for Lys, 120fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
E414A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E421A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E428D
-
8.5fold increase in Km-value for Lys, 1.8fold decrease in turnover number for Lys, 1.7fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
E428Q
-
2fold decrease in Km-value for Lys, 9fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
F261A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
F274A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
F426H
-
78fold increase in Km-value for Lys, 1.3fold decrease in turnover number for Lys, 1.6fold increase in Km-value for ATP, 5fold decrease in turnover number for ATP
F426W
-
6.2fold increase in Km-value for Lys, 3fold decrease in turnover number for Lys, 9.2fold increase in Km-value for ATP, 1.4fold decrease in turnover number for ATP
G216A
-
75fold increase in Km-value for Lys, 1.9fold increase in turnover number for Lys, 16fold increase in Km-value for ATP, 4.25fold decrease in turnover number for ATP
G265A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
H270A
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
I266A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
N260A
-
inactive
N263A
-
inactive
N271A
-
inactive
N424D
-
2fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 1.8fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
N424Q
-
20fold increase in Km-value for Lys, 2.8fold decrease in turnover number for Lys, 69fold increase in Km-value for ATP, 1.5fold decrease in turnover number for ATP
P272A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
R262A
-
inactive
R269A
-
inactive
R269E
-
inactive
R269K
-
inactive
R269Q
-
inactive
R480A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
S267A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
V268A
-
inactive
Y280F
-
9.2fold increase in Km-value for Lys, 58fold decrease in turnover number for Lys, 5.2fold increase in Km-value for ATP, 20fold decrease in turnover number for ATP
Y280S
-
44fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 3.9fold increase in Km-value for ATP, 9.7fold decrease in turnover number for ATP
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
truncated N-terminal tRNA anticodon-binding domain
TAB
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
DELTA1-65
-
mutant enzyme binds poorly to tRNALys, but does not increase tRNALys packaging into HIV-1 viruses
DELTA452-597
-
mutant enzyme binds to but does not aminoacylate tRNALys, still facilitates an increase in tRNALys packaging into virions
DELTAS70-T584
truncation at S70-T584 and full length LysRS (M1-V597) expressed, purified, and attempted for crystallization
E525K
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
F244A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
F244A/I245A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
hKRSDELTA1-24
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
hKRSDELTA24-42
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
hKRSDELTA60
removal of the amino-terminal extension
I245A
-
the mutant shows wild type aminoacylation activity
I246D
-
the mutant shows 60% aminoacylation activity compared to the wild type enzyme
I246D/R247A
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I250D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I250D/I251D
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I251D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D/R255A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
K249A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
R247A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
R255A
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
R438W
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
S248D
-
the mutant shows wild type aminoacylation activity
S248D/K249A
-
the mutant shows wild type aminoacylation activity
S270D
-
the mutant shows 800fold enhanced catalytic activity compared to the wild type enzyme, with enhanced diadenosine tetraphosphate synthetic activity, enhanced ATP hydrolysis and lost aminoacylation activity for tRNALys
Y491E
-
exhibits significant improvement compared to the wild type in aminoacylation of a tRNALysUUG
additional information