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
-
anti-synthetase
-
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
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Reaction
Reaction on EC 6.1.1.21 - histidine-tRNA ligase
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
two molecules of ATP and histidine are bound per molecule of enzyme
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
2-step mechanism, elucidation of structure-activity relationship, the N-terminal catalytic domain contains the six-stranded antiparallel beta-sheet and the three motifs characteristics of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, a C-terminal alpha/beta domain may be involved in the recognition of the anticodon stem and loop of tRNAHis
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
2-step mechanism, elucidation of structure-activity relationship, the N-terminal catalytic domain contains the six-stranded antiparallel beta-sheet and the three motifs characteristics of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, a C-terminal alpha/beta domain may be involved in the recognition of the anticodon stem and loop of tRNAHis
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
interaction mechanism of RNA substrate and enzyme, active site structure
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
mechanism, active site structure, ligand induced structural changes, highly cooperative dynamics
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
N73 is a discriminator base involved in histidylation activity, substrate recognition mechanism
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
substrate-assisted concerted mechanism, rate of aminoacyl transfer is independent of the interaction between the carboxamide group of Q127 and the alpha-carboxylate carbon
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
the major groove amine of C73 and the 6-keto oxygen of G-1 of tRNAHis participate in hydrogen bonding with histidine-tRNA ligase, while the 5'-monophosphate provides necessary electrostatic interactions with the positive residues of enzyme active site
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation
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ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation
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