Information on EC 6.1.1.3 - threonine-tRNA ligase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
6.1.1.3
-
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RECOMMENDED NAME
GeneOntology No.
threonine-tRNA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA charging
-
-
threonine metabolism
-
-
Aminoacyl-tRNA biosynthesis
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-threonine:tRNAThr ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-46-5
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
several strains, overview, gene thrS
-
-
Manually annotated by BRENDA team
overproducing strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS
-
-
Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Chloroadenosine 5'-triphosphate + L-threonine + tRNAThr
?
show the reaction diagram
ATP + 3-hydroxynorvaline + tRNAThr
AMP + diphosphate + 3-hydroxynorvalyl-tRNAThr
show the reaction diagram
-
the specificity constant kcat/KM for beta-hydroxynorvaline is only 20-30fold less than that of cognate threonine, amino acid activation is the potential rate-limiting step of b3-hydroxynorvaline aminoacylation
-
-
?
ATP + hydroxynorvaline + tRNAThr
AMP + diphosphate + hydroxynorvalyl-tRNAThr
show the reaction diagram
10-70% less active than with L-threonine
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
ATP + L-serine + tRNASer
?
show the reaction diagram
-
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.
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
show the reaction diagram
ATP + L-threonine + tRNA1Thr
AMP + diphosphate + L-threonyl-tRNA1Thr
show the reaction diagram
-
-
-
-
?
ATP + L-threonine + tRNA2Thr
AMP + diphosphate + L-threonyl-tRNA2Thr
show the reaction diagram
-
-
-
-
?
ATP + L-threonine + tRNAThr
?
show the reaction diagram
-
catalyzes the attachment of threonine onto its cognate tRNA molecule, prior to participation of the aminoacylated tRNA in the protein synthesis
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
Formycin 5'-triphosphate + L-threonine + tRNAThr
?
show the reaction diagram
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-serine + tRNASer
?
show the reaction diagram
-
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.
-
-
?
ATP + L-threonine + tRNA1Thr
AMP + diphosphate + L-threonyl-tRNA1Thr
show the reaction diagram
-
-
-
-
?
ATP + L-threonine + tRNA2Thr
AMP + diphosphate + L-threonyl-tRNA2Thr
show the reaction diagram
-
-
-
-
?
ATP + L-threonine + tRNAThr
?
show the reaction diagram
-
catalyzes the attachment of threonine onto its cognate tRNA molecule, prior to participation of the aminoacylated tRNA in the protein synthesis
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
additional information
?
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NH4+
-
partial activation
Phosphorus
-
phosphoprotein containing phosphoserine, activity can be modulated by reversible phosphorylation
Rb+
-
partial activation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
2'-deoxyadenosine 5'-triphosphate
-
-
2'-O-Methyladenosine 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
3'-O-Methyladenosine 5'-triphosphate
-
-
5'-O-[N-(threonyl)-sulfamoyl] adenosine
Borrelidin
hydrogen peroxide
-
oxidizes cysteine182 residue critical for editing, which leads to Ser-tRNAThr formation and protein mistranslation that impaired growth of Escherichia coli. Presence of major heat shock proteases is required to allow cell growth in medium containing serine and hydrogen peroxide, which suggests that the mistranslated proteins are misfolded
operator mRNA domain 2
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-
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Purineriboside 5'-triphosphate
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tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
threonyl-AMP
tubercidin 5'-triphosphate
-
-
Zn2+
-
inhibits the editing reaction
additional information
-
reactive oxygen species cause editing defect and misacylation by WT ThrRS
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
spermine
additional information
-
3-hydroxynorvaline enhances the ATPase function of the synthetic site, at a rate not increased by nonaminoacylatable tRNA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
2-Chloroadenosine 5'-triphosphate
0.267 - 0.387
ATP
0.5
Formycin 5'-triphosphate
1.95 - 7
hydroxynorvaline
25 - 142
L-serine
0.00003 - 0.897
L-threonine
0.00189
threonine
-
-
0.00013 - 0.00095
tRNA1Thr
-
0.00027 - 0.0014
tRNA2Thr
-
0.00003 - 0.179
tRNAThr
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42 - 90
ATP
21 - 22
hydroxynorvaline
1.3 - 30
L-serine
0.64 - 90
L-threonine
0.53
RNAThr
-
tRNAThr of E. coli
-
1.73
threonyl-tRNA
-
-
0.033 - 0.118
tRNA1Thr
-
0.01 - 0.103
tRNA2Thr
-
0.00157 - 0.7
tRNAThr
0.037 - 0.23
tRNAThr of Thermus thermophilus
-
-
-
additional information
additional information
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
L-serine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
11.18
L-threonine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
1.093 - 171.7
tRNAThr
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002262 - 0.05
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
0.0000039 - 0.000091
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
0.000083 - 0.00582
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
0.0331 - 0.193
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
0.05
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
0.000034 - 0.000399
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
0.0000225 - 0.000588
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
0.0000011 - 0.0000041
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
0.0000027 - 0.000032
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
0.00002 - 0.000463
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
0.000089 - 0.002242
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
0.0000029 - 0.0000107
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
0.000039 - 0.001518
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
0.0000003 - 0.05
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
0.0000093 - 0.000072
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
0.0000009 - 0.0000033
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
0.0000007 - 0.000003
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
0.00014 - 0.000935
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
0.05
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
0.000004 - 0.0000095
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
0.0000006 - 0.0000024
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
0.0000028 - 0.0000134
5'-O-[N-(threonyl)-sulfamoyl] adenosine
0.000004 - 0.006
Borrelidin
0.000132 - 0.05
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
additional information
additional information
-
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
presteady-state, assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
presteady-state, assay at
50
-
assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cell line LCC-RK1
Manually annotated by BRENDA team
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cell line CRL-1781
Manually annotated by BRENDA team
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parental GAT- and borrelidin-resistant 2000A
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
association of the enzyme with high MW cellular component
-
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6600
-
ThrRS-dual targeting peptide, determined by SDS-PAGE
30860
-
predicted from cDNA
45000
-
predicted from cDNA
53120
-
predicted from cDNA
63110
-
predicted from cDNA
76000
-
2 * 76000, SDS-PAGE
77000
-
2 * 77000, SDS-PAGE under denaturing conditions
82000
-
2 * 82000, SDS-PAGE
85000
-
2 * 85000, SDS-PAGE
86000
-
2 * 86000, SDS-PAGE
150000
154000
-
sedimentation equilibrium measurement
164000
-
PAGE at different gel concentrations
170000
-
gel filtration
195000
-
mitochondrial, gel filtration
206000
-
cytoplasmic, gel filtration
additional information
-
nucleotide and deduced amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information