6.1.1.3: threonine-tRNA ligase
This is an abbreviated version!
For detailed information about threonine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.3
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6.1.1.3
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synthetases
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aminoacyl-trna
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aminoacylation
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threonylation
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anticodon
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aarss
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borrelidin
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phenylalanyl-trna
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isoacceptors
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misactivates
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noncognate
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alanyl-trna
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mischarged
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anticodon-binding
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hisrs
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anticodon-like
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mistranslation
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post-transfer
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diagnostics
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drug development
- 6.1.1.3
- synthetases
- aminoacyl-trna
- aminoacylation
-
threonylation
-
anticodon
-
aarss
- borrelidin
- phenylalanyl-trna
-
isoacceptors
-
misactivates
-
noncognate
- alanyl-trna
-
mischarged
-
anticodon-binding
- hisrs
-
anticodon-like
-
mistranslation
-
post-transfer
- diagnostics
- drug development
Reaction
Synonyms
ApThrRS-1, ApThrRS-2, BaThrRS, EcThrRS, ectRNAThr, McThrRS, mitochondrial threonyl-tRNA synthetase, MJ1197, MmThrRS, More, Mst1, ScmtThrRS, SfThrRS-1, SfThrRS-2, Synthetase, threonyl-transfer ribonucleate, TarS, Thr-tRNA synthetase, Threonine translase, Threonine--tRNA ligase, Threonine-transfer ribonucleate synthetase, threonyl tRNA synthetase, Threonyl-ribonucleic synthetase, Threonyl-transfer ribonucleate synthetase, Threonyl-transfer ribonucleic acid synthetase, Threonyl-transfer RNA synthetase, Threonyl-tRNA synthetase, ThrRS, ThrRS1, ThrS, TRS
ECTree
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Metals Ions
Metals Ions on EC 6.1.1.3 - threonine-tRNA ligase
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K+
Mg2+
Ni2+
the enzyme can bind one Ni2+ per subunit, binding of nickel inhibits the oxidation of enzyme residue Cys182 by H2O2 or air
Phosphorus
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phosphoprotein containing phosphoserine, activity can be modulated by reversible phosphorylation
Zn2+
Mg2+
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Mg2+ can be substituted by Ca2+ and Mn2+. Zn2+ and Ni2+ can only very poorly replace Mg2+
Zn2+
mediates amino acid discrimination of the enzyme, located in the active site, formation of a pentacoordinate intermediatewith both the amino group and the side chain hydroxyl of L-threonine
Zn2+
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used to discriminate against the isosteric valine at the activation step
Zn2+
the enzyme can bind one Zn2+ per subunit, crystal structure analysis, PDB ID 1EVK, residues C334, H385 and H511 coordinate a zinc ion, which is essential for aminoacylation. Binding of zinc inhibits the oxidation of enzyme residue Cys182 by H2O2 or air
Zn2+
the presence of dynamically rigid zinc ion coordination sphere and bipartite mode of recognition of ectRNAThr are observed
Zn2+
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zinc binding in the catalytic site, the active site zinc atom is essential for the recognition of threonine, three amino acids forming the zinc-binding site, overview