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
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threonylation
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anticodon
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aarss
- borrelidin
- phenylalanyl-trna
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isoacceptors
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misactivates
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noncognate
- alanyl-trna
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mischarged
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anticodon-binding
- hisrs
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anticodon-like
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mistranslation
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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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Natural Substrates Products
Natural Substrates Products on EC 6.1.1.3 - threonine-tRNA ligase
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REACTION DIAGRAM
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
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?
ATP + L-serine + tRNASer
?
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yeast mitochondrial threonyl-tRNA synthetase MST1 lacks an editing domain and utilizes pre-transfer editing to discriminate against serine. MST1 misactivates serine and edits seryl adenylate (Ser-AMP) in the absence of the cognate tRNA. MST1 hydrolyzes 80% of misactivated Ser-AMP at a rate 4fold higher than that for the cognate threonyl adenylate (Thr-AMP) while releasing 20% of Ser-AMP into the solution.
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?
ATP + L-threonine + tRNA1Thr
AMP + diphosphate + L-threonyl-tRNA1Thr
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?
ATP + L-threonine + tRNA2Thr
AMP + diphosphate + L-threonyl-tRNA2Thr
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ATP + L-threonine + tRNAThr
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catalyzes the attachment of threonine onto its cognate tRNA molecule, prior to participation of the aminoacylated tRNA in the protein synthesis
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?
AMP + diphosphate + L-seryl-tRNAThr
Mesomycoplasma mobile
reaction of EC 6.1.1.11, mischarging of tRNAThr, low activity
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-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
Mesomycoplasma mobile ATCC 43663
reaction of EC 6.1.1.11, mischarging of tRNAThr, low activity
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?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
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reaction of EC 6.1.1.11, mischarging of tRNAThr
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?
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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-
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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-
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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-
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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-
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
regulatory mechanism
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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the enzyme acts as both an enzyme and a regulator of gene expression, it aminoacylates tRNAThr isoacceptors and binds to its own mRNA, inhibiting its translation, overview
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile ATCC 43663
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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?
AMP + diphosphate + L-threonyl-tRNAThr1
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?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
Saccharomyces cerevisiae ATCC 204508 / S288c
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?
AMP + diphosphate + L-threonyl-tRNAThr2
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?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
Saccharomyces cerevisiae ATCC 204508 / S288c
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?
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interaction of the dual targeting peptide of Thr-tRNA synthetase with the chloroplastic receptor Toc34 in Arabidopsis thaliana as a function of AtToc34 concentration. Mapping the AtToc34 interaction sites in AtThrRS-dTP(2-60), overview
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additional information
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interaction of the dual targeting peptide of Thr-tRNA synthetase with the chloroplastic receptor Toc34 in Arabidopsis thaliana as a function of AtToc34 concentration. Mapping the AtToc34 interaction sites in AtThrRS-dTP(2-60), overview
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?
additional information
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aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
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?
additional information
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regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme
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?
additional information
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the enzyme needs to discriminate between threonine, serine, and valine in vivo, mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution, overview
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additional information
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a freestanding proofreading domain is required for protein synthesis quality control in archaea
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additional information
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structure-based evolutionary considerations
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additional information
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aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
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?
additional information
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a freestanding proofreading domain is required for protein synthesis quality control in archaea
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additional information
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a freestanding proofreading domain is required for protein synthesis quality control in archaea
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additional information
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no activity with L-Val, L-Ala, or L-Cys
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additional information
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ScmtThrRS exhibits a tRNA-dependent pre-transfer editing activity that is specific for the tRNAThr2 isoacceptor, whereas tRNAThr1 is unable to stimulate such activity. Editing capability of tRNAThr1 with requirement for the presence of an editing domain
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additional information
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ScmtThrRS exhibits a tRNA-dependent pre-transfer editing activity that is specific for the tRNAThr2 isoacceptor, whereas tRNAThr1 is unable to stimulate such activity. Editing capability of tRNAThr1 with requirement for the presence of an editing domain
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?
additional information
?
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Saccharomyces cerevisiae ATCC 204508 / S288c
ScmtThrRS exhibits a tRNA-dependent pre-transfer editing activity that is specific for the tRNAThr2 isoacceptor, whereas tRNAThr1 is unable to stimulate such activity. Editing capability of tRNAThr1 with requirement for the presence of an editing domain
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?