6.1.1.16: cysteine-tRNA ligase
This is an abbreviated version!
For detailed information about cysteine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.16
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6.1.1.16
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synthetases
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aminoacyl-trnas
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aminoacylation
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cys-trnacys
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prolyl-trna
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prors
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seprs
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cysteinyl-trnacys
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asnrs
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atp-ppi
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ilers
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valrs
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o-phosphoseryl-trna
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maripaludis
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aarss
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sep-trna:cys-trna
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sepcyss
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o-phosphoserine
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drug development
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molecular biology
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medicine
- 6.1.1.16
- synthetases
- aminoacyl-trnas
- aminoacylation
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cys-trnacys
-
prolyl-trna
- prors
- seprs
-
cysteinyl-trnacys
- asnrs
-
atp-ppi
- ilers
- valrs
-
o-phosphoseryl-trna
- maripaludis
-
aarss
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sep-trna:cys-trna
- sepcyss
- o-phosphoserine
- drug development
- molecular biology
- medicine
Reaction
Synonyms
CarS, CARS1, CARS2, class I CysRS, class I cysteinyl-tRNA synthetase, CRS, CysRS, cysS, Cysteine translase, Cysteine--tRNA ligase, cysteine-specific aminoacyl-tRNA synthetase, cysteinyl tRNA synthetase, Cysteinyl-transfer ribonucleate synthetase, Cysteinyl-transfer RNA synthetase, Cysteinyl-tRNA synthetase, MSMEG_6074, Synthetase, cysteinyl-transfer ribonucleate
ECTree
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Engineering
Engineering on EC 6.1.1.16 - cysteine-tRNA ligase
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C209S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0031% of the wild-type ratio
C28S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.012% of the wild-type ratio
C28S/C209S
C28S/C209S/H234N/E238Q
C36S/C214S/C244S
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site-directed mutagenesis, activity is similar to the wild-type enzyme, but the affinity for cysteine binding is increased
DELTA288-461
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the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 7% of the wild-type ratio
DELTA328-461
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the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 0.32% of the wild-type ratio, aminoacylation of tRNACys is not detectable
E354Q
E354Q/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 22fold relative to the wild type enzyme
H206S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 60% of the wild-type ratio
H224N/H235N
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.042% of the wild-type ratio
H224S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 5.7% of the wild-type ratio
H234N/E238Q
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0059% of the wild-type ratio
H234S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.015% of the wild-type ratio
H235S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.38% of the wild-type ratio
H238S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 30% of the wild-type ratio
H256S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.4fold relative to the wild type enzyme
H404A/R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 209fold relative to the wild type enzyme
H40A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 204fold relative to the wild type enzyme
M294A
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.7fold relative to the wild type enzyme
M294A/H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 8.1fold relative to the wild type enzyme
M294A/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 370fold relative to the wild type enzyme
N351D
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.25% of the wild-type ratio
R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 291fold relative to the wild type enzyme
R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 1.5fold relative to the wild type enzyme
V27E
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mutation does not affect the discrimination of the enzyme for serine. 4fold increase in Km-value for cysteine and 9fold reduction of turnover number for ATP
W205F
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.55% of the wild-type ratio
W205Y
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site-directed mutagenesis, highly reduced activity, highly increased Km for cysteine
D239A/D240A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D417A/E420A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D435A/D436A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D239A/D240A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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D417A/E420A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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D435A/D436A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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E217del
the mutation leads to a severe epileptic encephalopathy and complex movement disorder
P251L
the mutation leads to a severe epileptic encephalopathy and complex movement disorder
additional information
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site-directed mutagenesis, no ATP-diphosphate exchange activity, residual aminoacylation activity
C28S/C209S
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0026% of the wild-type ratio
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site-directed mutagensis, mutation of all zinc binding ligands, complete loss of bound zinc, weak ability to bind serine, thus loss of amino acid substrate discrimination ability
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the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
E354Q
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 6.8fold relative to the wild type enzyme
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construction of a Co2+-substituted wild-type enzyme, similar properties as the Zn2+-wild-type enzyme but slightly reduced activity
additional information
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construction of a fusion of a eukaryote-specific domain of human CysRS enabling recognition of the sequence differences in the tertiary core of tRNACys. The fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals
additional information
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deletion of the halophilic-specific peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, maintaining the peptide length but substituting acidic residues in the peptide with neutral or basic residues has no major deleterious effect, suggesting that the acidity of the peptide is not important for the kcat of tRNA aminoacylation, construction of point mutants and deletion mutants, e.g. deletion mutant DELTA193-212, overview
additional information
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deletion of the halophilic-specific peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, maintaining the peptide length but substituting acidic residues in the peptide with neutral or basic residues has no major deleterious effect, suggesting that the acidity of the peptide is not important for the kcat of tRNA aminoacylation, construction of point mutants and deletion mutants, e.g. deletion mutant DELTA193-212, overview
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additional information
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construction of a DELTAC mutant of the enzyme that terminates at V642, removing residues 643 to 748 from the full-length enzyme, the mutant enzymes shows increased activity in the first amino acid activation step and reduced activity in the second aminoacylation step compared to the wild-type full-length enzyme
additional information
construction of a cysS gene disruption knockout mutant, which is viable under normal growth conditions
additional information
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construction of a cysS gene disruption knockout mutant, which is viable under normal growth conditions
additional information
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generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
Mycolicibacterium smegmatis mc2155 / ATCC 700084
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generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
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