6.1.1.19: arginine-tRNA ligase
This is an abbreviated version!
For detailed information about arginine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.19
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6.1.1.19
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aminoacyl-trna
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synthetases
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aminoacylation
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arginylation
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anticodon
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pontocerebellar
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aarss
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isoacceptors
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glnrs
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atp-ppi
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multisynthetase
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lysyl-trna
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trnaasp
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l-canavanine
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glutaminyl-trna
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aspartyl-trna
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isoleucyl
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phenylalanyl-trna
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glutamyl-prolyl-trna
- 6.1.1.19
- aminoacyl-trna
- synthetases
- aminoacylation
-
arginylation
-
anticodon
-
pontocerebellar
-
aarss
-
isoacceptors
- glnrs
-
atp-ppi
-
multisynthetase
- lysyl-trna
- trnaasp
- l-canavanine
- glutaminyl-trna
- aspartyl-trna
-
isoleucyl
- phenylalanyl-trna
-
glutamyl-prolyl-trna
Reaction
Synonyms
Arg-tRNA synthetase, Arginine translase, Arginine--tRNA ligase, Arginine-tRNA synthetase, Arginyl transfer ribonucleic acid synthetase, Arginyl-transfer RNA synthetase, Arginyl-tRNA synthetase, arginyl–tRNA synthetase, ArgRS, ArgS2, MtArgRS, RARS, RARS2, RRS, Synthetase, arginyl-transfer ribonucleate
ECTree
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Engineering
Engineering on EC 6.1.1.19 - arginine-tRNA ligase
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C599Y
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expression in Saccharomices cerevisiae, shows reduced activity and stability
DELTA1-73
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KM-value for tRNAArg is 1.2fold higher than the wild-type value, turnover number is 1.4fold higher
argS MA5002
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mutant argS MA5002 differs from the wild-type ArgRS structural gene by one mutation, a substitution of an Arg by a Ser at position 134. It exhibits a 4times to 6times as low activity and a 5times as high Km value for ATP as the wild-type enzyme in aminoacylation and ATP-diphosphate exchange, Km values for Arg and tRNAArg remain unaltered
M460V
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mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
Y313A
the mutation results in a merely 2fold reduction in binding affinity
Y524D
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mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
DELTANhcArgRS
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N-terminal 72-amino acid deletion mutant with higher specific activity than the wild type enzyme
RARSL
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the RARSL mutation in the mitochondrial arginyl–tRNA synthetase gene is associated with pontocerebellar hypoplasia
additional information
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2 mutant enzymes with reduced affinity for Arg, one mutant with reduced affinity for arginine-tRNAArg and reduced aminoacylation in vivo for two of the five isoaccepting species of tRNAArg
additional information
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biosynthetic preparation of an enzyme where Trp are replaced by 4-fluorotryptophane
additional information
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isolation of 26 mutants by random mutagenesis