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
6.1.1.3 threonine-tRNA ligaseAdvanced search results
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results (Engineering
Engineering on EC 6.1.1.3 - threonine-tRNA ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Q502R
identification of the zebrafish cq16 mutant gene encoding threonyl-tRNA synthetase (tars) with a missense mutation. The abnormal branching of intersegmental vessels is caused by the increased expression of vascular endothelial growth factor A (vegfa) in tarscq16 mutant. Inhibition of Vegf signaling suppresses the abnormal vascular branching observed in tarscq16 mutant
C182A
site-directed mutagenesis, the mutation leads to loss of editing activity and to Ser misacylation to tRNAThr. C182A and C182S mutations reduce the kcat value of editing over 500fold
C182S
site-directed mutagenesis, the mutation leads to loss of editing activity and to Ser misacylation to tRNAThr. C182A and C182S mutations reduce the kcat value of editing over 500fold
D180A
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charging of tRNAThr with serine, mutant is no longer able to rapidly deacetylate Ser-tRNAThr
D435A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
D46E
site-directed mutagenesis, the mutant has a modest reduction in its aminoacylation activity compared to wild-type, and its post-transfer editing activity is abolished
D46E/H186G
site-directed mutagenesis, the mutant EcThrRS strongly supports growth of a yeast thrS deletion strain (ScDELTAthrS)
D46E/Y173F
site-directed mutagenesis, the mutant EcThrRS supports growth of a yeast thrS deletion strain (ScDELTAthrS)
D46E/Y173H
site-directed mutagenesis, the mutant does not support growth of a yeast thrS deletion strain (ScDELTAthrS)
D46E/Y173K
site-directed mutagenesis, the mutant does not support growth of a yeast thrS deletion strain (ScDELTAthrS)
D46E/Y173R
site-directed mutagenesis, the mutant does not support growth of a yeast thrS deletion strain (ScDELTAthrS)
D46E/Y173S
site-directed mutagenesis, the mutant does not support growth of a yeast thrS deletion strain (ScDELTAthrS)
D46R
site-directed mutagenesis, the mutant has a modest reduction in its aminoacylation activity compared to wild-type, and its post-transfer editing activity is abolished
D549A
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modified interation of anticodon loop/C-ter domain, activity similar to the wild-type
E458D
site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, mutant shows decreased apparent rate constants
E600A
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modified interation of anticodon loop/C-ter domain, 710fold increased activity
G459D
site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, mutant shows decreased apparent rate constants
H186A
site-directed mutagenesis, the mutant does not show oxidation of Cys182 by H2O2 and only partially by NaOCl
H186G
site-directed mutagenesis, the mutant EcThrRS strongly supports growth of a yeast thrS deletion strain (ScDELTAthrS)
H309A
site-directed mutagenesis, mutant shows highly increased Ki for inhibitor borrelidin compared to the wild-type enzyme
H337A
site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme
H73A
H73A/H309A
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis
H73A/H77A
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charging of tRNAThr with serine, mutant is no longer able to deacetylate Ser-tRNAThr
H77A
site-directed mutagenesis, the mutant shows oxidation of Cys182 by H2O2 and NaOCl
K136A
site-directed mutagenesis, the mutant EcThrRS supports growth of a yeast thrS deletion strain (ScDELTAthrS)
K136E
site-directed mutagenesis, the mutant does not support growth of a yeast thrS deletion strain (ScDELTAthrS)
K136R
site-directed mutagenesis, the mutant EcThrRS supports growth of a yeast thrS deletion strain (ScDELTAthrS)
K246A
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modified interation of acceptor stem and catalytic domain, 2.9fold increased activity
K249A
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modified interation of acceptor stem and catalytic domain, 3.5fold increased activity
K577A
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modified interation of anticodon loop/C-ter domain, 118fold increased activity
L489W
site-directed mutagenesis, mutant has a reduced space of the hydrophobic cluster near the active site resulting in a 1500fold increase in Ki for inhibitor borrelidin compared to the wild-type enzyme
N324A
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modified interation of cross-subunit contacts, 3.5fold increased activity
N502A
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modified interation of cross-subunit contacts, 2.1fold increased activity
N575A
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modified interation of anticodon loop/C-ter domain, 9.4fold increased activity
P296A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
P296S
site-directed mutagenesis, mutant shows slightly increased Ki for inhibitor borrelidin compared to the wild-type enzyme
P335A
site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme
P424K
site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, the mutant shows decreased apparent rate constants
P464A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
R282A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
R349A
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modified interation of cross-subunit contacts, 42fold increased activity
S347A
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modified interation of cross-subunit contacts, similar to the wild-type
S367A
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modified interation of acceptor stem and catalytic domain, 11fold increased activity
S429A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
T307A
site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme
W434Y
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reduced activity, Trp434 is involved in conformational changes during substrate binding
Y173D
site-directed mutagenesis, the mutant has a modest reduction in its aminoacylation activity compared to wild-type, and its post-transfer editing activity is abolished
Y173R
site-directed mutagenesis, the mutant has a modest reduction in its aminoacylation activity compared to wild-type, and its post-transfer editing activity is abolished
Y205F
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modified interation of acceptor stem and N-terminal domain, 7.7fold increased activity
Y219F
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modified interation of acceptor stem and N-terminal domain, similar to the wild-type
Y313A
site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme
Y348F
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modified interation of cross-subunit contacts, 6.5fold increased activity
H385A
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site-directed mutagenesis, the mutant shows altered substrate specificity, overview
H385N
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site-directed mutagenesis, the mutant shows altered substrate specificity, overview
H385Y
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site-directed mutagenesis, the mutant shows altered substrate specificity, overview
R583H
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site-directed mutagenesis, the mutant shows altered substrate specificity, overview
H9A/H13A
Mesomycoplasma mobile
site-directed mutagenesis, the post-transfer editing of MmThrRS mutant H9A/H13A is reduced compared with that of wild-type MmThrRS, the in vivo mutation of more crucial residues is required to abolish the post-transfer editing
H9A/H13A/K86A/D117A/C119A/H123A
Mesomycoplasma mobile
site-directed mutagenesis, the post-transfer editing of mutant MmThrRS-N2M is completely lost
H9A/H13A
Mesomycoplasma mobile ATCC 43663
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site-directed mutagenesis, the post-transfer editing of MmThrRS mutant H9A/H13A is reduced compared with that of wild-type MmThrRS, the in vivo mutation of more crucial residues is required to abolish the post-transfer editing
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H9A/H13A/K86A/D117A/C119A/H123A
Mesomycoplasma mobile ATCC 43663
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site-directed mutagenesis, the post-transfer editing of mutant MmThrRS-N2M is completely lost
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E134A
site-directed mutagenesis, the mutation has no effect on the deacylation activity
H83A
site-directed mutagenesis, the mutant possesses the editing activity albeit with a slower rate compared to the wild-type enzyme
K121M
site-directed mutagenesis, substitution of Lys121 to serine does not abolish Ser-tRNAThr deacylation activity
K121S
site-directed mutagenesis, substitution of Lys121 to serine results in a complete abolition of Ser-tRNAThr deacylation activity
M129K
site-directed mutagenesis, the mutant shows binding not only to L-serine but also to a variety of other L-amino acids that are tested in addition to binding to various D-amino acids, overview
Y120A
site-directed mutagenesis, the mutation has no effect on the deacylation activity
D423A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D437A
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the mutant shows strongly increased catalytic efficiency compared to the wild type enzyme
E401A
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the mutant shows strongly increased catalytic efficiency compared to the wild type enzyme
K408A
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the mutant shows about wild type catalytic efficiency for tRNAThr1
K440A
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
N356A
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
N359A
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
N400A
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
N432A
R439A
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the mutant shows weaker binding for tRNAThr1 and displays increased Km for tRNAThr2 as well
S409E
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the mutant shows about wild type catalytic efficiency for tRNAThr1
additional information
H73A
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis
H73A
site-directed mutagenesis, the mutant does not show oxidation of Cys182 by H2O2 and NaOCl
N432A
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N432A
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the mutant shows weaker binding for tRNAThr1 and displays increased Km for tRNAThr2 as well
additional information
construction of a truncated enzyme: core domain DELTAN comprising residues 242-642
additional information
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construction of a truncated enzyme: core domain DELTAN comprising residues 242-642
additional information
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construction of chromosomal disruption null mutant strain with no activity, construction of a truncated mutant lacking the N1 and N2 domains, 93.5fold increased activity
additional information
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truncated lamdaN-enzyme mutant, lacking the N-terminal domains N1 and N2, produces Ser-tRNAThr, reduced activity and altered substrate recognition compared to the wild-type which does nearly not incorporate serine
additional information
truncated lamdaN-enzyme mutant, lacking the N-terminal domains N1 and N2, produces Ser-tRNAThr, reduced activity and altered substrate recognition compared to the wild-type which does nearly not incorporate serine
additional information
the mutant EcThrRS-DELTAN1 lacking domain N1 shows no post-transfer editing activity
additional information
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the mutant EcThrRS-DELTAN1 lacking domain N1 shows no post-transfer editing activity
additional information
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mutations of any of the three amino acids forming the zinc-binding site inactivate the enzyme and have a dominant negative effect on growth if the corresponding genes are placed on a multicopy plasmid, not due to the formation of inactive heterodimers, the titration of tRNAThr by an inactive enzyme, or its misaminoacylation but is, rather, due to the regulatory function of threonyl-tRNA synthetase, overview, the mutations confer a dominant lethal phenotype, overproduction of the inactive enzyme represses the expression of the wild-type chromosomal copy of the gene to an extent incompatible with bacterial growth, phenotypes, overview
additional information
construction of mutants consisting of catalytic or editing enzyme domains, overview
additional information
the albinic las mutant is selected from an MNU-mutagenized population of indica cultivar N22, transgenic rice lines are produced by Agrobacterium tumefaciens-mediated co-cultivation. Albinic plants die at the fourth leaf stage presumably as seed nutrient reserves becomes exhausted, phenotype, overview. Expression levels of class I genes (PsbD1, PsaA1, PsaA2 and RBCL) in the las mutant are sharply reduced compared to wild type, class II genes (NADH2, NADH4, ATPCFalpha) are expressed normally, and expressions of class III genes (RpoA, RpoB, RpoC1 and RpoC2) are increased compared to wild-type. NEP accumulates in the las mutant, whereas those of genes transcribed by PEP are impaired. Phenotype, overview
additional information
construction of mutants consisting of catalytic or editing enzyme domains, overview, construction of mutant strain PBL205 with a disruption of gene thrS, i.e. SSO3004-3050
additional information
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construction of mutants consisting of catalytic or editing enzyme domains, overview, construction of mutant strain PBL205 with a disruption of gene thrS, i.e. SSO3004-3050
additional information
a minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading, complementation of a ScmtThrRS gene knockout strain. Construction of the gene encoding the chimeric Saccharomyces cerevisiae cytoplasmic-mitochondrial ThrRS (CmThrRS), overview. Role of the tRNAThr1 anticodon in editing by CmThrRS. The MST1 gene knockout strain, ScDELTAMST1, reveals that aminoacylation and tRNA binding domains co-evolved to acquire tRNAThr1 recognition capability
additional information
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a minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading, complementation of a ScmtThrRS gene knockout strain. Construction of the gene encoding the chimeric Saccharomyces cerevisiae cytoplasmic-mitochondrial ThrRS (CmThrRS), overview. Role of the tRNAThr1 anticodon in editing by CmThrRS. The MST1 gene knockout strain, ScDELTAMST1, reveals that aminoacylation and tRNA binding domains co-evolved to acquire tRNAThr1 recognition capability
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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a minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading, complementation of a ScmtThrRS gene knockout strain. Construction of the gene encoding the chimeric Saccharomyces cerevisiae cytoplasmic-mitochondrial ThrRS (CmThrRS), overview. Role of the tRNAThr1 anticodon in editing by CmThrRS. The MST1 gene knockout strain, ScDELTAMST1, reveals that aminoacylation and tRNA binding domains co-evolved to acquire tRNAThr1 recognition capability
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