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6.1.1.2: tryptophan-tRNA ligase

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

Word Map on EC 6.1.1.2

Reaction

ATP
+
L-tryptophan
 +
tRNATrp
=
AMP
 +
diphosphate
 +
L-tryptophyl-tRNATrp

Synonyms

(Mt)TrpRS, BsTRpRS, drTrpRS II, EcTrpRS, hTrpRS, hWRS, IFP53, mini tryptophanyl-tRNA synthetase, mini-TrpRS, More, Synthetase, tryptophanyl-transfer ribonucleate, T2-TrpRS, Trp-RS, TrpRS, TrpRS II, TrpRS Urzyme, TrpRS1, TrpRS2, Tryptophan translase, Tryptophan--tRNA ligase, Tryptophanyl ribonucleic synthetase, tryptophanyl tRNA synthase, tryptophanyl tRNA synthetase, Tryptophanyl-transfer ribonucleate synthetase, Tryptophanyl-transfer ribonucleic acid synthetase, Tryptophanyl-transfer ribonucleic synthetase, Tryptophanyl-transfer RNA synthetase, Tryptophanyl-tRNA synthase, Tryptophanyl-tRNA synthetase, tryptophanyl-tRNA synthetase II, tryptophanyl-tRNA synthetase1, tryptophanyl-tRNA synthetase2, trytophanyl-tRNA synthetase, tyrosyl tRNA synthetase, WARS, WARS2, WRS

ECTree

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

Engineering

Engineering on EC 6.1.1.2 - tryptophan-tRNA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E153D
-
ratio of turnover number to Km-value for ATP is 109% of wild-type value, ratio of turnover number to Km-value for Trp is 114% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 89% of wild-type value
E153G
-
no detectable activity in activation of Trp unless tRNATRp is added to the reaction
E153K
-
ratio of turnover number to Km-value for ATP is 79% of wild-type value, ratio of turnover number to Km-value for Trp is 68% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 3% of wild-type value
K149D/E153R
-
ratio of turnover number to Km-value for ATP is 30% of wild-type value, ratio of turnover number to Km-value for Trp is 10% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 1% of wild-type value
K149E
-
ratio of turnover number to Km-value for ATP is 99.7% of wild-type value, ratio of turnover number to Km-value for Trp is 89% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 37% of wild-type value
K149G
-
ratio of turnover number to Km-value for ATP is 111% of wild-type value, ratio of turnover number to Km-value for Trp is 88% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 55% of wild-type value
K149R
-
ratio of turnover number to Km-value for ATP is 112% of wild-type value, ratio of turnover number to Km-value for Trp is 98% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 64% of wild-type value
V144P
-
mutant selectively aminoacylates the cognate mutant opal suppressor tRNATrp(UCA) with 5-hydroxy-L-tryptophan and not with any endogenous amino acid
W92A
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
W92F
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
W92Q
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
E438A
-
TrpRS single mutant
R135H
-
TrpRS single mutant
R135H/E438A
-
TrpRS double mutant, binds with Zn2+ or heme to enhance its aminoacylation activity
H445E
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q107K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q146K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q411K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
D146A
-
site-directed mutagensis, the mutant shows highly reduced activity compared to the wild-type enzyme
A310W
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
A7D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
D382-TIEEHR-Q389
deletion of the tRNA anticodon-binding domain insertion, consisting of eight residues in the human TrpRS, abolishes the apoptotic activity of the enzyme for endothelial cells, whereas its translational catalysis and cell-binding activities remain unchanged
D99A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99E
site-directed mutagenesis, the mutant shows slightly reduced activity and kcat compared to the wild-type enzyme
D99K
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99V
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
E11L
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
E35G
site-directed mutagenesis, the mutant shows similar induction of TNF-alpha and MIP-1alpha production compared to wild-type
E451Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
G161W
T2-TrpRS mutant, tryptophan pocket is blocked by the bulky indole side chain of the tryptophan introduced at position 161, angiostatic activity involves the tryptophan and adenosine pockets
G172M
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
H129A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H130R
H140A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H170A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H173A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H257A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H336A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H375A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H387A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H445A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H73A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
I311E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
I311V
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
K102A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102R
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
K114Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K153Q
site-directed mutagenesis, the human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin
K418Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K431A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431R
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
L10D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L22G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L9D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
M42D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N152G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N30G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q145G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q194A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Q194L
site-directed mutagenesis, the mutant is inactive
R106A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106K
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
T18G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
V85A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction
V85A/V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85K
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85K mutant has barely detectable aminoacylation activity
V85L
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85L mutant is able to acylate bovine tRNATrp with very high effciency
V85S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows no activity in the ATP-diphosphate exchange reaction, but retains aminoacylation activity
V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
V90S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
Y159A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Y159A/Q194A
T2-TrpRS mutant, enzyme specific recognition of the indole nitrogen of tryptophan is disrupted, angiostatic activity involves the tryptophan and adenosine pockets
Y159F
site-directed mutagenesis, the mutant shows slightly reduced activity and reduce kcat compared to the wild-type enzyme
H48N
-
naturally occuring mutation of TrpRS2
H48Q
-
naturally occuring mutation of TrpRS2
TrpRS2(H48N)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(H48Q)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F/H48Q)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F/Q13K)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(Q13K)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A/H48Q]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A/L9F]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T/H48Q]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T/L9F]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T]
-
locus mutant, constructed for analysing the indolmycin resistance
H48N
-
naturally occuring mutation of TrpRS2
-
H48Q
-
naturally occuring mutation of TrpRS2
-
additional information