6.1.1.21: histidine-tRNA ligase
This is an abbreviated version!
For detailed information about histidine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.21
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6.1.1.21
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synthetases
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aminoacylation
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aminoacyl-trna
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autoantibody
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histidylation
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myositis
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anti-jo-1
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polymyositis
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anticodon
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dermatomyositis
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aarss
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perrault
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hiss
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histidinol
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anti-synthetase
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guanylyltransferase
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hsd17b4
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myositis-specific
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c10orf2
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thrrs
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threonyl-trna
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trna-like
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acid-starved
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seryl-trna
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analysis
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medicine
- 6.1.1.21
- synthetases
- aminoacylation
- aminoacyl-trna
- autoantibody
-
histidylation
- myositis
-
anti-jo-1
- polymyositis
-
anticodon
- dermatomyositis
-
aarss
-
perrault
- hiss
- histidinol
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anti-synthetase
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guanylyltransferase
- hsd17b4
-
myositis-specific
- c10orf2
- thrrs
- threonyl-trna
-
trna-like
-
acid-starved
- seryl-trna
- analysis
- medicine
Reaction
Synonyms
antihistidyl-tRNA synthetase, class II histidyl-tRNA synthetase, HARS, HARS1, HARS2, HisRS, HisRS-1, HisRS-2, Histidine translase, Histidine--tRNA ligase, Histidine--tRNA ligase homolog, histidine-tRNA ligase, histidine-tRNA ligase homolog, histidyl tRNA synthetase, Histidyl-transfer ribonucleate synthetase, histidyl-transfer RNA synthetase, Histidyl-tRNA synthetase, HRS, HTS1, Jo-1, Jo-1 antigen, mitochondrial histidyl tRNA synthetase, Synthetase, histidyl-transfer ribonucleate
ECTree
6.1.1.21 histidine-tRNA ligaseAdvanced search results
results (
results (Engineering
Engineering on EC 6.1.1.21 - histidine-tRNA ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C88V/C196S/C241L
denoted as clHisRS, can not be labeled with maleimide probes
L276C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
L402C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
MDCC-HisRS
fluorescently labeled version of HisRS, conjugated with 7-diethylamino-3-((((2-maleimidyl)ethyl)amino)carbonyl)-coumarin, MDCC, to a cysteine introduced at residue 212, located in the insertion domain
N212C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
N368C clHisRS
an additional cysteine is introduced at a solvent-accessible position proximal to substrate binding sites
NcatHisRS
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320-residue fragment, NcatHisRS, truncated immediately following motif 3 catalyzes both the the specific aminoacylation of tRNA and ATP-diphosphate exchange, albeit less efficiently than the full length enzyme. NcatHisRs shows no mischarging of noncognate tRNAs but exhibits reduced selectivity for the C73 discriminator base. NcatHisRs is monomeric, indicating that the C-terminal domain is essential for maintaining the dimeric structure of the enzyme
Q118E
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site-directed point mutagenesis of an active site residue, reduced kcat but unaltered Km with wild-type tRNAHis G-1
R116A
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site-directed mutagenesis, reduced activity, increased specificity for the wild-type full length tRNAHis G-1
R123A
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site-directed point mutagenesis of an active site residue, reduced activity, increased specificity for the wild-type full length tRNAHis G-1
R259H
R9H
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site-directed point mutangenesis, increased activity with wild-type full length tRNAHis G-1, reduced activity with the synthetic tRNAHis G-1 and A-1 substrates, increased specificity for the wild-type full length tRNAHis G-1
V-HisRS-R259K
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mutants: V-HisRS-R259K, V-HisRS-R259Q, des(A2-G10)-HisRS, des(A2-Q6)-HisRS, V-His-RS with N-terminal addition of valine, and M-HisRS with N-terminal addition of methionine. N-terminal addition of either methionine or valine, or the deletion of 6 amino terminal amino acids deceases the specific aminoacylation activity 2fold to 7fold. Further N-terminal deletions of 10 or 17 amino acids causes 100fold reduced aminoacylation and 10fold reduced ATP-diphosphate exchange. Removal of 18 or more amino acids from the N-terminus results in an inactive enzyme mutants. The two point mutations R259Q and R259K, show blocked histidyl-tRNA synthetase activity without affecting histidine or ATP binding
D175E
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
D364Y
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
D48A
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site-directed mutagenesis, the mutant is cleaved by caspase-6, but not by granzyme B
L200V
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naturally occuring mutations in HARS2 involved in the Perrault syndrome, the mutant shows reduced activity compared to wild-type enzyme
P134H
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
R137Q
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
S356N
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
T132I
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
V155G
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
V368L
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naturally occuring mutations in HARS2 involved in the Perrault syndrome, the mutant shows reduced activity compared to wild-type enzyme
Y330C
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the mutant with reduced aminoacylation activity is associated with Charcot-Marie-Tooth disease type 2W
Y454S
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the mutation is associated with childhood deafness, blindness, and episodic hallucinations during acute illness
additional information
R259H
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mutant Arg259His, with 1000fold decreased second order rate constant kcat/Km for the ATP-diphosphate exchange, and 500fold decreased kcat/Km for aminoacylation
additional information
construction of GFP-fusion proteins with the first 71 amino acids of the enzyme sequence, transformation of and expression in Nicotiana tabacum protoplasts, functional targeting to the mitochondria and chloroplasts of tobacco
additional information
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construction of GFP-fusion proteins with the first 71 amino acids of the enzyme sequence, transformation of and expression in Nicotiana tabacum protoplasts, functional targeting to the mitochondria and chloroplasts of tobacco
additional information
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RNAi-dependent downregulation of hars-1, embryos from wild-type animals are laid onto bacteria expressing double-stranded RNA and the progeny are exposed to RNAi throughout development
additional information
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construction of four minimal, active site fragments, urzymes, of Escherichia coli class II HisRS by PCR-based subcloning, the fragments comprise: HisRS1 residues 16-134, HisRS2 residues 10-134, HisRS3 residues 16-134 and 301-320, and HisRS4 residues 10-134 and 301-320. HisRS-3 binds ATP far more tightly and histidine less strongly than native, full-length HisRS or its intact catalytic domain. HisRS-3 urzyme steady-state kinetic parameters differ substantially from those of native full-length HisRS. All urzymes show relative rate enhancements compared to the wild-type enzyme, overview
additional information
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HisRS granzyme B site mapping using site-directed mutagenesis
additional information
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identification of a deletion mutant HARS2 DELTA200-211, probably involved in the Perrault syndrome, that is not stably expressed in mammalian mitochondria, its also shows no dimerization
additional information
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construction of Egr1 null or defect mutants affects HisRS genes, Egr1, Zif268, is an immediate early gene encoding an inducible transcription factor involved in synaptic plasticity and several forms of memory in rodents, allelic differences between mouse strains can introduce variations in differential proteomic analyses of genetically modified organisms
additional information
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mutational study of the 1:73 base pair recognition by yeats HisRS using two chemically synthesized 24-nucleotide RNA microhelices, overview
additional information
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overexpression in Escherichia coli, as a fusion protein containing additional 15 amino acids
