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2-Chloroadenosine 5'-triphosphate + L-threonine + tRNAThr
?
AMP + diphosphate + L-threonyl-tRNAThr
ATP + L-threonine + tRNAThr
-
-
-
-
r
ATP + 3-hydroxynorvaline + tRNAThr
AMP + diphosphate + 3-hydroxynorvalyl-tRNAThr
-
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
10-70% less active than with L-threonine
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
ATP + L-serine + tRNASer
?
-
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
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
ATP + L-threonine + tRNA1Thr
AMP + diphosphate + L-threonyl-tRNA1Thr
-
-
-
-
?
ATP + L-threonine + tRNA2Thr
AMP + diphosphate + L-threonyl-tRNA2Thr
-
-
-
-
?
ATP + L-threonine + tRNAThr
?
-
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
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
Formycin 5'-triphosphate + L-threonine + tRNAThr
?
additional information
?
-
2-Chloroadenosine 5'-triphosphate + L-threonine + tRNAThr
?
-
-
-
-
?
2-Chloroadenosine 5'-triphosphate + L-threonine + tRNAThr
?
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
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
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
-
-
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
low activity
-
-
r
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
1000fold less active than with L-threonine
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
-
very low activity with the wild-type enzyme
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
Mesomycoplasma mobile
reaction of EC 6.1.1.11, mischarging of tRNAThr, low activity
-
-
?
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
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
L-serine is a poor substrate for the wild-type enzyme
-
-
r
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
-
reaction of EC 6.1.1.11, mischarging of tRNAThr
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
secondary structure of the tRNAThr, enzyme utilizes substrates from archaeon with discriminator base U73 and Escherichia coli with discriminator base A73
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme from Aeropyrum pernix threonylated threonine tRNAs from Aeropyrum pernix, Haloferax volcanii and Escherichia coli
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme recognizes the first three base pairs of acceptor stem in addition to the second and the third letters of anticodon of tRNA(Thr). The discriminator base is not involved in recognition by the enzyme
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme threonylates not only archaeal (Aeropyrum pernix and Haloferax volcanii) threonine tRNAs but also Escherichia coli threonine tRNA
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme from Aeropyrum pernix threonylated threonine tRNAs from Aeropyrum pernix, Haloferax volcanii and Escherichia coli
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme threonylates not only archaeal (Aeropyrum pernix and Haloferax volcanii) threonine tRNAs but also Escherichia coli threonine tRNA
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the enzyme recognizes the first three base pairs of acceptor stem in addition to the second and the third letters of anticodon of tRNA(Thr). The discriminator base is not involved in recognition by the enzyme
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
tRNA aminoacylation
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
regulatory mechanism
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
via AMP-L-threonine-enzyme intermediate in a two-step process
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
for cognate threonine, amino acid activation is likely to be the rate-limiting step. The inability of wild-type ThrRS to prevent utilization of beta-hydroxynorvaline as a substrate illustrates that the naturally occurring enzyme lacks the capability to effectively discriminate against nonproteogenic amino acids that are not encountered under normal physiological conditions
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Escherichia coli ectRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
tRNAThr3 of Escherichia coli
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
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
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the zinc atom in the active site is essential for the recognition of threonine
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
secondary structure of the tRNAThr, specific for archaeal tRNAThr with discriminator base U73, no activity with one of Escherichia coli with discriminator base A73
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
Escherichia coli threonine tRNA is not aminoacylated by the Haloferax volcanii enzyme. The Escherichia coli mutant tRNAThr having U73 is threonylated by the Haloferax volcanii enzyme. The discriminator base U73 of Haloferax volcanii tRNAThr is a strong determinant for the recognition by threonyl-tRNA synthetase
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile ATCC 43663
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
determination of substrate binding sites, catalytic sites, and catalytic mechanism
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
editing mechanism
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
the main chains atoms of Tyr119 and Tyr120 are sufficient to prevent the deacylation of Thr-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
MST1 can attach threonine to both tRNAThr1 and the regular tRNAThr2, but not to the wild-type tRNAHis. But a loss of the first nucleotide G-1 in tRNAHis converts it to a substrate for MST1
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
substrate binding induces conformational changes
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
tRNAThr of Thermus thermophilus
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
tRNAThr of Thermus thermophilus
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
specific binding mode of mitochondrial tRNAThr1 to mitochondrial ScmtThrRS
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
specific binding mode of mitochondrial tRNAThr1 to mitochondrial ScmtThrRS
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
-
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
-
-
-
?
Formycin 5'-triphosphate + L-threonine + tRNAThr
?
-
-
-
-
?
Formycin 5'-triphosphate + L-threonine + tRNAThr
?
-
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
enzyme also has a regulatory function by binding the so-called operator site located in the leader of its own mRNA and thereby inhibits translational initiation by competing with ribosome binding
-
?
additional information
?
-
no activity with L-valine, determination of amino acid activation and discriminating editing mechanism
-
?
additional information
?
-
the enzyme represses the translation of its own mRNA by binding to an operator located upstream of the initiation codon thereby using the recognition mode of the tRNA anticodon loop to initiate binding
-
?
additional information
?
-
-
the enzyme represses the translation of its own mRNA by binding to an operator located upstream of the initiation codon thereby using the recognition mode of the tRNA anticodon loop to initiate binding
-
?
additional information
?
-
-
regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme
-
?
additional information
?
-
the enzyme needs to discriminate between threonine, serine, and valine in vivo, mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution, overview
-
-
?
additional information
?
-
-
in the pre-steady state, asymmetric activation of cognate threonine and noncognate serine is observed in the active sites of dimeric ThrRS, with similar rates of activation. In the absence of tRNA, seryl-adenylate is hydrolyzed 29old faster by the ThrRS catalytic domain than threonyl-adenylate. The rate of seryl transfer to cognate tRNA is only 2fold slower than threonine
-
-
?
additional information
?
-
the interaction of ecRNAThr with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme
-
-
?
additional information
?
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
the N-terminal enzyme domain is responsible for editing
-
-
?
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
?
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
?
additional information
?
-
-
structure-based evolutionary considerations
-
-
?
additional information
?
-
-
enzyme can interact with high-MW RNAs
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
mischarging of the enzyme with noncognate amino acids, overview, post-transfer editing mechanism of the D-aminoacyl-tRNA deacylase-like domain in the archaeal threonyl-tRNA synthetase, mechanistic insights into the removal of noncognate L-serine from tRNAThr, M129 is responsible for enantiomeric selection in DTD, Glu134 is involved in fixing the seryl moiety in the active site, overview
-
-
?
additional information
?
-
-
mischarging of the enzyme with noncognate amino acids, overview, post-transfer editing mechanism of the D-aminoacyl-tRNA deacylase-like domain in the archaeal threonyl-tRNA synthetase, mechanistic insights into the removal of noncognate L-serine from tRNAThr, M129 is responsible for enantiomeric selection in DTD, Glu134 is involved in fixing the seryl moiety in the active site, overview
-
-
?
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
?
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
?
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
?
additional information
?
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
L-serine is a poor substrate for the wild-type enzyme, the N-terminal enzyme domain is responsible for editing
-
-
?
additional information
?
-
-
L-serine is a poor substrate for the wild-type enzyme, the N-terminal enzyme domain is responsible for editing
-
-
?
additional information
?
-
-
the enzyme examines side chain structures of amino acids in 4 recognition steps. For each step the enzyme uses special distinct structures or conformations of the binding cleft
-
-
?
additional information
?
-
-
specificity with regard to amino acids, discrimination factors
-
-
?
additional information
?
-
-
addition of first nucleotide G-1 to tRNAThr1 allows efficient histidylation by histidyl-tRNA synthetase
-
-
?
additional information
?
-
-
no activity with L-Val, L-Ala, or L-Cys
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
residues Gln180 and Gln292 are important in cofactor binding
-
-
?
additional information
?
-
the enzyme, mitochondrial ThrRS (ScmtThrRS), catalyzes the aminoacylation of tRNAThr1 and tRNAThr2, U33a and G36 of tRNAThr1 are critical nucleotides for aminoacylation by ScmtThrRS. tRNAThr1 stimulates pre-transfer editing in the presence of an editing domain
-
-
?
additional information
?
-
-
the enzyme, mitochondrial ThrRS (ScmtThrRS), catalyzes the aminoacylation of tRNAThr1 and tRNAThr2, U33a and G36 of tRNAThr1 are critical nucleotides for aminoacylation by ScmtThrRS. tRNAThr1 stimulates pre-transfer editing in the presence of an editing domain
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme, mitochondrial ThrRS (ScmtThrRS), catalyzes the aminoacylation of tRNAThr1 and tRNAThr2, U33a and G36 of tRNAThr1 are critical nucleotides for aminoacylation by ScmtThrRS. tRNAThr1 stimulates pre-transfer editing in the presence of an editing domain
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
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
?
-
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 + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
ATP + L-threonine + tRNA1Thr
AMP + diphosphate + L-threonyl-tRNA1Thr
-
-
-
-
?
ATP + L-threonine + tRNA2Thr
AMP + diphosphate + L-threonyl-tRNA2Thr
-
-
-
-
?
ATP + L-threonine + tRNAThr
?
-
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
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
additional information
?
-
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
Mesomycoplasma mobile
reaction of EC 6.1.1.11, mischarging of tRNAThr, low activity
-
-
?
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
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
-
reaction of EC 6.1.1.11, mischarging of tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
regulatory mechanism
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
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
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Mesomycoplasma mobile ATCC 43663
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
-
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
-
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme
-
?
additional information
?
-
the enzyme needs to discriminate between threonine, serine, and valine in vivo, mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution, overview
-
-
?
additional information
?
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
-
structure-based evolutionary considerations
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
?
additional information
?
-
-
no activity with L-Val, L-Ala, or L-Cys
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
H2O2
oxidation of ThrRS by H2O2 causes editing defects and Ser misincorporation at Thr codons due to oxidation of Cys182, zinc or nickel ions inhibit C182 oxidation by hydrogen peroxide. Reducing the oxidized ThrRS with DTT or sodium arsenite (NaAsO2) recovers the editing activity, cysteine residue C182 is reversibly oxidized
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
-
-
Purineriboside 5'-triphosphate
-
-
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
tubercidin 5'-triphosphate
-
-
ZINC27215482
-
docking analysis, overview. The best inhibitor, which can be used to develop novel drugs against bovine brucellosis
Zn2+
inhibits the editing reaction
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
-
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
-
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
(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-(1-oxoisoindolin-5-yl)-phenyl)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-(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-((3-(3-methyl-1H-indazol-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-((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-((4-phenoxyphenyl)sulfonyl)-butanamide
-
-
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)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-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
-
-
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)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'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
-
-
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
-
(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-hydroxy-4-methylpentanamide
-
-
(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-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-hydroxybutanamide
-
-
(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-hydroxybutanamide
-
-
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
-
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
-
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
(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-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
-
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
(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-(1-aminoisoquinolin-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-(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-(2,4-diaminoquinazolin-7-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-(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-(3-chloro-1H-indazol-5-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-(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-chloroquinazolin-7-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-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-amino-2-methylquinazolin-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-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-((3-(4-aminoquinazolin-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-((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-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
-
-
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)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)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
-
-
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-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-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
-
-
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
-
(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)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
-
(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)-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
-
-
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-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
-
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
-
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
-
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
-
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
-
borrelidin
-
inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
borrelidin
-
predicted binding mode of borrelidin, BaThrRS enzyme homology structure model docking of the ligand, overview
borrelidin
slowly but tight binding, noncompetitive with respect to threonine and ATP, inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
borrelidin
is an 18-membered macrolide polyketide produced by several actinomycete bacteria of the Streptomyces spp.. Identification of borrelidin binding site on threonyl-tRNA synthetase, molecular docking, overview. Borrelidin binds the pocket outside but adjacent to the active site of ThrRS, consisting of residues Y313, R363, R375, P424, E458, G459, and K465. Borrelidin may induce the cleft closure, which blocks the release of Thr-AMP and phosphate, to inhibit activity of ThrRS rather than inhibit the binding of ATP and threonine
borrelidin
-
inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
borrelidin
-
inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
borrelidin
-
inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
borrelidin
-
inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
-
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
-
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
-
threonyl-AMP
-
-
additional information
-
the BaThrRS-binding site structure for inhibitors is analyzed. Virtual database screening for inhibitors of the enzyme using docking studies, free energy of binding between BaThrRS and inhibitors, overview
-
additional information
-
reactive oxygen species cause editing defect and misacylation by WT ThrRS
-
additional information
development of novel borrelidin derivatives and rational design of structure-based ThrRS inhibitors, overview
-
additional information
-
development of novel borrelidin derivatives and rational design of structure-based ThrRS inhibitors, overview
-
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0.4
2-Chloroadenosine 5'-triphosphate
0.5
Formycin 5'-triphosphate
1.95 - 7
hydroxynorvaline
0.00003 - 4.4
L-threonine
0.00013 - 0.00095
tRNA1Thr
-
0.00027 - 0.0014
tRNA2Thr
-
0.00045
tRNAThr1
pH 8.5, 30°C, recombinant enzyme
-
additional information
additional information
-
0.4
2-Chloroadenosine 5'-triphosphate
-
-
0.4
2-Chloroadenosine 5'-triphosphate
-
ATP
0.267
ATP
-
wild-type enzyme, pH 7.2, 37°C
0.387
ATP
-
mutant enzyme W434Y, pH 7.2, 37°C
0.5
Formycin 5'-triphosphate
-
-
0.5
Formycin 5'-triphosphate
-
threonine
1.95
hydroxynorvaline
pH 7.2, 37°C, wild-type enzyme
7
hydroxynorvaline
pH 7.2, 37°C, truncated enzyme DELTAN
25
L-serine
pH 7.2, 60°C, recombinant wild-type enzyme
55
L-serine
pH 7.2, 60°C, recombinant wild-type enzyme
81.5
L-serine
pH 7.2, 37°C, wild-type enzyme
120
L-serine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
142
L-serine
pH 7.2, 37°C, truncated enzyme DELTAN
582.37
L-serine
-
pH 7.5, 30°C
939.72
L-serine
Mesomycoplasma mobile
pH 7.5, 30°C
0.00003
L-threonine
-
wild-type enzyme complementing the null mutant
0.09
L-threonine
-
pH 7.5, 65°C, wild-type enzyme
0.1
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
0.1
L-threonine
-
pH 7.5, 55°C, wild-type enzyme
0.1
L-threonine
-
pH 7.5, 65°C, wild-type enzyme
0.101
L-threonine
pH 7.4, 30°C, recombinant mutant G459D
0.104
L-threonine
pH 7.4, 30°C, recombinant mutant E458D
0.105
L-threonine
pH 7.4, 30°C, recombinant wild-type enzyme
0.108
L-threonine
pH 7.4, 30°C, recombinant mutant P424K
0.11
L-threonine
pH 7.5, 37°C, wild-type enzyme
0.11
L-threonine
pH 7.2, 37°C, wild-type enzyme
0.11
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
0.18
L-threonine
pH 7.2, 37°C, truncated enzyme DELTAN
0.201
L-threonine
-
wild-type enzyme, pH 7.2, 37°C
0.3
L-threonine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
0.897
L-threonine
-
mutant enzyme W434Y, pH 7.2, 37°C
3.39
L-threonine
-
pH 7.5, 30°C
4.4
L-threonine
Mesomycoplasma mobile
pH 7.5, 30°C
0.00013
tRNA1Thr
-
mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.0002
tRNA1Thr
-
mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00024
tRNA1Thr
-
mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00024
tRNA1Thr
-
mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00028
tRNA1Thr
-
mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00029
tRNA1Thr
-
wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.0003
tRNA1Thr
-
mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.0003
tRNA1Thr
-
mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00031
tRNA1Thr
-
mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00031
tRNA1Thr
-
mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00046
tRNA1Thr
-
mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00047
tRNA1Thr
-
mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00048
tRNA1Thr
-
mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00049
tRNA1Thr
-
mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00059
tRNA1Thr
-
mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00083
tRNA1Thr
-
mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00095
tRNA1Thr
-
mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00027
tRNA2Thr
-
mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00037
tRNA2Thr
-
mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00044
tRNA2Thr
-
mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00044
tRNA2Thr
-
wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00049
tRNA2Thr
-
mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00051
tRNA2Thr
-
mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00059
tRNA2Thr
-
mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00064
tRNA2Thr
-
mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00069
tRNA2Thr
-
mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00078
tRNA2Thr
-
mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00083
tRNA2Thr
-
mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00094
tRNA2Thr
-
mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00123
tRNA2Thr
-
mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00139
tRNA2Thr
-
mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.0014
tRNA2Thr
-
mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00003
tRNAThr
wild-type enzyme
0.000037 - 0.00007
tRNAThr
-
of Thermus thermophilus, , depending on temperature
0.00005
tRNAThr
-
of E. coli
0.00014
tRNAThr
-
of E. coli
0.00029
tRNAThr
-
pH 7.2, 37°C, tRNAThr1, MST1
0.00043
tRNAThr
truncated enzyme core DELTAN
0.00044
tRNAThr
-
pH 7.2, 37°C, tRNAThr2, MST1
0.0015
tRNAThr
-
pH 7.2, 37°C, ThrRS, aminoacylation with Thr
0.0015
tRNAThr
-
pH 7.2, 37°C, tRNAThr1(G-1), MST1
additional information
additional information
-
-
-
additional information
additional information
-
Km values of variants of tRNAThr transcripts
-
additional information
additional information
-
kinetics and kinetic mechanism
-
additional information
additional information
-
mutant enzymes complementing the null mutant
-
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes with threonine and serine
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes with threonine and serine
-
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes with threonine and serine
-
additional information
additional information
presteady-state and steady-state kinetic measurement
-
additional information
additional information
-
presteady-state and steady-state kinetic measurement
-
additional information
additional information
-
steady-state kinetic measurement
-
additional information
additional information
-
steady-state kinetic measurement
-
additional information
additional information
-
steady-state kinetic measurement
-
additional information
additional information
-
steady-state kinetic measurement
-
additional information
additional information
-
kinetics of diphosphate exchange activities and threonylation of tRNAThr of ThrRS with or without H2O2 treatment, overview
-
additional information
additional information
-
kinetics of MST1 with different tRNAs, overview
-
additional information
additional information
-
pre-steady-state kinetics, kinetics of ATPase activity in presence of 3-hydroxynorvaline, overview
-
additional information
additional information
aminoacylation kinetics of ScmtThrRS for various tRNAThr1 mutants derived from U33a or G36, overview. Rate constants of AMP formation by chimeric mutant enzyme CmThrRS
-
additional information
additional information
-
aminoacylation kinetics of ScmtThrRS for various tRNAThr1 mutants derived from U33a or G36, overview. Rate constants of AMP formation by chimeric mutant enzyme CmThrRS
-
additional information
additional information
enzyme kinetics and stopped-flow fluorescence analysis, Michaelis-Menten steady-state kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
enzyme kinetics and stopped-flow fluorescence analysis, Michaelis-Menten steady-state kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of the enzyme for cognate Thr and noncognate Ser are determined with an ATP-phosphate exchange reaction
-
additional information
additional information
Mesomycoplasma mobile
kinetics of the enzyme for cognate Thr and noncognate Ser are determined with an ATP-phosphate exchange reaction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.73
L-threonyl-tRNAThr
-
-
0.0338
tRNAThr1
pH 8.5, 30°C, recombinant enzyme
-
additional information
additional information
-
42
ATP
-
mutant enzyme W434Y, pH 7.2, 37°C
90
ATP
-
wild-type enzyme, pH 7.2, 37°C
21
hydroxynorvaline
pH 7.2, 37°C, truncated enzyme DELTAN
22
hydroxynorvaline
pH 7.2, 37°C, wild-type enzyme
0.55
L-serine
Mesomycoplasma mobile
pH 7.5, 30°C
1.15
L-serine
-
pH 7.5, 30°C
1.3
L-serine
pH 7.2, 60°C, recombinant wild-type enzyme
1.83
L-serine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
12.3
L-serine
pH 7.2, 60°C, recombinant wild-type enzyme
26
L-serine
pH 7.2, 37°C, wild-type enzyme
30
L-serine
pH 7.2, 37°C, truncated enzyme DELTAN
0.64
L-threonine
-
wild-type enzyme complementing the null mutant
1.2
L-threonine
-
pH 7.5, 65°C, wild-type enzyme
1.9
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
2 - 8
L-threonine
pH 7.4, 30°C, recombinant mutant G459D
2.16
L-threonine
Mesomycoplasma mobile
pH 7.5, 30°C
3 - 6
L-threonine
pH 7.2, 37°C, wild-type enzyme
3.32
L-threonine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
3.8
L-threonine
-
pH 7.5, 65°C, wild-type enzyme
6.08
L-threonine
-
wild-type enzyme complementing the null mutant
6.31
L-threonine
-
pH 7.5, 30°C
13.5
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
16
L-threonine
-
pH 7.5, 55°C, wild-type enzyme
30
L-threonine
-
mutant enzyme W434Y, pH 7.2, 37°C
30
L-threonine
pH 7.4, 30°C, recombinant mutant P424K
33
L-threonine
pH 7.5, 37°C, wild-type enzyme
34
L-threonine
pH 7.4, 30°C, recombinant mutant E458D
35
L-threonine
pH 7.4, 30°C, recombinant wild-type enzyme
37
L-threonine
pH 7.2, 37°C, truncated enzyme DELTAN
90
L-threonine
-
wild-type enzyme, pH 7.2, 37°C
0.033
tRNA1Thr
-
mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.05
tRNA1Thr
-
mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.05
tRNA1Thr
-
mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.05
tRNA1Thr
-
mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.05
tRNA1Thr
-
wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.053
tRNA1Thr
-
mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.055
tRNA1Thr
-
mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.06
tRNA1Thr
-
mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.067
tRNA1Thr
-
mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.073
tRNA1Thr
-
mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.08
tRNA1Thr
-
mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.082
tRNA1Thr
-
mutant enzyme Y405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.087
tRNA1Thr
-
mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.093
tRNA1Thr
-
mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.112
tRNA1Thr
-
mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.117
tRNA1Thr
-
mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.118
tRNA1Thr
-
mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.01
tRNA2Thr
-
mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.017
tRNA2Thr
-
mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.03
tRNA2Thr
-
mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.038
tRNA2Thr
-
wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.04
tRNA2Thr
-
mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.043
tRNA2Thr
-
mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.045
tRNA2Thr
-
mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.045
tRNA2Thr
-
mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.053
tRNA2Thr
-
mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.058
tRNA2Thr
-
mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.06
tRNA2Thr
-
mutant enzyme Y405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.067
tRNA2Thr
-
mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.088
tRNA2Thr
-
mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.1
tRNA2Thr
-
mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.103
tRNA2Thr
-
mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
-
0.00157
tRNAThr
-
pH 7.2, 37°C, tRNAThr1(G-1), MST1
0.0383
tRNAThr
-
pH 7.2, 37°C, tRNAThr2, MST1
0.0467
tRNAThr
-
pH 7.2, 37°C, tRNAThr1, MST1
0.05
tRNAThr
-
pH 7.2, 37°C, ThrRS, aminoacylation with Thr
0.21
tRNAThr
-
tRNAThr of E. coli
0.52 - 0.7
tRNAThr
-
tRNAThr of Thermus thermophilus
0.53
tRNAThr
-
tRNAThr of E. coli
additional information
additional information
-
-
-
additional information
additional information
-
mutant enzymes complementing the null mutant
-
additional information
additional information
-
rate constants for adenylate synthesis by ThrRS in the absence of tRNA, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
0.0000034 - 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
-
0.002262
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.01258
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
Ki above 0.05 mM with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
-
Ki above 0.05 mM with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000039
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000074
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000077
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000091
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000083
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000127
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000143
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.00582
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0331
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0365
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0368
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.193
(2S,3R)-2-amino-3-hydroxy-N-((4-phenoxyphenyl)sulfonyl)-butanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-3-hydroxy-N-methyl-N-((3-(1-oxoisoindolin-5-yl)phenyl)sulfonyl)butanamide
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000034
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.00007
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000136
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000399
(2S,3R)-2-amino-N'-(3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)-3-hydroxybutanehydrazide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000225
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000324
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000601
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000588
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000011
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000018
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000027
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000041
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000027
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000043
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000141
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000032
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxypentanamide
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.00002
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000023
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000025
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000463
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000089
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.00009
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000115
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.002242
(2S,3R)-2-amino-N-((3-(1-aminoisoquinolin-6-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000029
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000082
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000101
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000107
(2S,3R)-2-amino-N-((3-(2,4-diaminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000039
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000052
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000077
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.001518
(2S,3R)-2-amino-N-((3-(3-chloro-1H-indazol-5-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000003
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000007
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000008
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000012
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-2-amino-N-((3-(4-amino-2-chloroquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000093
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000122
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000172
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000072
(2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)-phenyl)sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000009
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000022
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000029
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000033
(2S,3R)-2-amino-N-((3-(4-aminoquinazolin-7-yl)phenyl)-sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000007
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000002
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000027
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000003
(2S,3R)-2-amino-N-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.00014
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000329
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000436
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000935
(2S,3R)-2-amino-N-(3-(4-amino-2-chloroquinazolin-7-yl)-benzyl)-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
-
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
(2S,3R)-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)sulfonyl)-2,3-dihydroxybutanamide
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000004
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000052
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000057
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3,4-dihydroisoquinolin-2(1H)-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
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
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000006
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000018
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000018
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000024
(2S,3R)-N-((7-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-2-amino-3-hydroxybutanamide
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000028
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000098
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000131
5'-O-[N-(threonyl)-sulfamoyl] adenosine
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000134
5'-O-[N-(threonyl)-sulfamoyl] adenosine
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.0000034
borrelidin
pH 7.4, 30°C, recombinant wild-type enzyme
0.000004
borrelidin
pH 7.5, 37°C, wild-type enzyme
0.0000045
borrelidin
-
pH 7.5, 55°C, wild-type enzyme
0.0000191
borrelidin
pH 7.4, 30°C, recombinant mutant E458D
0.0000651
borrelidin
pH 7.4, 30°C, recombinant mutant P424K
0.0001114
borrelidin
pH 7.4, 30°C, recombinant mutant G459D
0.006
borrelidin
-
above, pH 7.5, 65°C, wild-type enzyme
0.006
borrelidin
-
above, pH 7.5, 65°C, wild-type enzyme
0.006
borrelidin
pH 7.5, 37°C, mutant L489W
0.000132
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000164
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.000182
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
-
with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
0.05
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication
additional information
additional information
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additional information
additional information
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evolution
-
evolutionary development of unusual tRNAThr1, containing an enlarged 8-nt anticodon loop, which is required to reassign CUN codons from leucine to threonine, tRNAThr phylogenetic analysis, overview. MST1 has co-evolved with tRNAThr, which evoled from tRNAHis
evolution
-
tRNAThr phylogenetic analysis, overview
evolution
crucial importance of the only absolutely conserved residue within the N1 domain in regulating post-transfer editing activityand editing active sites by mediating an N1-N2 domain interaction in Escherichia coli ThrRS. Translational quality control of various ThrRSs and the role of the N1 domain in translational fidelity, overview
evolution
-
sequence comparison of threonyl-tRNA synthetases from Brucella abortus (BaThrRS) and Escherichia coli (EThrRS), which reveals 51% sequence identity
evolution
the catalytic core and tRNA binding domain of ScmtThrRS co-evolved to recognize the unusual tRNAThr1. Loss of the editing domain occurred at a very early stage in the evolution of yeast, while mitochondrial tRNALeu(CUN) reassignment was a more recent event. The 34UAG36 anticodon is harbored by mitochondrial tRNALeu(CUN) in other organisms, such as humans and even the yeasts Schizosaccharomyces pombe, Candida albicans. tRNALeu(CUN) has been consistently lost in the Saccharomyces cerevisiae mitochondrion during the evolution of the 24 mitochondrial tRNA genes. tRNAThr1 is not derived from the lost tRNALeu (CUN) but from tRNAHis with a 34GUG36 anticodon
evolution
the enzyme belongs to the class II of aminoacyl-tRNA sythetases
evolution
-
ThrRSs from Mycoplasma species exhibit differences in their domain composition and editing active sites compared with the canonical ThrRSs. The Mycoplasma capricolum ThrRS, which harbors an N1 domain and a degenerate N2 domain, is editing-defective, and is thus not capable to support the growth of a yeast thrS deletion strain (ScDELTAthrS). Translational quality control of various ThrRSs and the role of the N1 domain in translational fidelity, overview. McThrRS has lost its post-transfer editing activity, probably because of its degenerate editing active site in the N2 domain. MmThrRS has negligible tRNA-dependent pretransfer editing capacities
evolution
Mesomycoplasma mobile
ThrRSs from Mycoplasma species exhibit differences in their domain composition and editing active sites compared with the canonical ThrRSs. The Mycoplasma mobile ThrRS, the first example of a ThrRS naturally lacking the N1 domain, displays efficient post-transfer editing activity. Mycoplasma mobile ThrRS is able to support the growth of a yeast thrS deletion strain (ScDELTAthrS). Translational quality control of various ThrRSs and the role of the N1 domain in translational fidelity, overview
evolution
-
the catalytic core and tRNA binding domain of ScmtThrRS co-evolved to recognize the unusual tRNAThr1. Loss of the editing domain occurred at a very early stage in the evolution of yeast, while mitochondrial tRNALeu(CUN) reassignment was a more recent event. The 34UAG36 anticodon is harbored by mitochondrial tRNALeu(CUN) in other organisms, such as humans and even the yeasts Schizosaccharomyces pombe, Candida albicans. tRNALeu(CUN) has been consistently lost in the Saccharomyces cerevisiae mitochondrion during the evolution of the 24 mitochondrial tRNA genes. tRNAThr1 is not derived from the lost tRNALeu (CUN) but from tRNAHis with a 34GUG36 anticodon
-
evolution
Mesomycoplasma mobile ATCC 43663
-
ThrRSs from Mycoplasma species exhibit differences in their domain composition and editing active sites compared with the canonical ThrRSs. The Mycoplasma mobile ThrRS, the first example of a ThrRS naturally lacking the N1 domain, displays efficient post-transfer editing activity. Mycoplasma mobile ThrRS is able to support the growth of a yeast thrS deletion strain (ScDELTAthrS). Translational quality control of various ThrRSs and the role of the N1 domain in translational fidelity, overview
-
malfunction
-
reactive oxygen species cause editing defect and misacylation by WT ThrRS. H2O2-induced Ser-tRNAThr formation causes protein mistranslation
malfunction
identification of the zebrafish cq16 missense mutant Q502R presenting the disorganized vessels with abnormal branching of the established intersegmental vessels (ISVs) as well as aberrant patterning of the brain vascular network after 50 h post fertilization. The mutation in cq16 mutant gene encoding threonyl-tRNA synthetase (tars) is responsible for the phenotype. The abnormal branching of ISVs 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. The mutation in tars leads to ISV abundant sprouting in zebrafish. Injection of human TARS mRNA potently reduces the vascular aberrant branching in tarscq16 mutant
malfunction
mutation of threonyl-tRNA synthetase results in a lethal albinic rice mutant las. las mutant plants show weak chlorophyll fluorescence, negligible chlorophyll accumulation, and defective thylakoid membrane development. Chloroplast-encoded protein levels are sharply reduced in the las mutant. Biogenesis of chloroplast rRNAs (16S and 23S rRNA) is arrested, leading to impaired translation and protein synthesis. 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. The plastid ribosomal RNA biogenesis system is abnormal in las plants. Phenotype, overview
malfunction
threonyl-tRNA synthetase (ThrRS) misactivates serine and utilizes an editing site cysteine (C182 in Escherichia coli) to hydrolyze Ser-tRNAThr. Hydrogen peroxide oxidizes C182, leading to SertRNAThr production and mistranslation of threonine codons as serine. C182 is oxidized to sulfenic acid by air, hydrogen peroxide, and hypochlorite. Air oxidation increases the Ser-tRNAThr level in the presence of elongation factor Tu. C182 forms a putative metal binding site with three conserved histidine residues (H73, H77, and H186). H73 and H186, but not H77, are critical for activating C182 for oxidation. Zinc or nickel ions inhibit C182 oxidation by hydrogen peroxide. Bacteria may use ThrRS editing to sense the oxidant levels in the environment. C182 oxidation modeling, overview. C182 is directly activated by H73 and H186 rather than by a metal ion. Chronic oxidative stress leads to ThrRS mistranslation in vivo
malfunction
threonyl-tRNA synthetase overexpression correlates with angiogenic markers and progression of human ovarian cancer
malfunction
-
reactive oxygen species cause editing defect and misacylation by WT ThrRS. H2O2-induced Ser-tRNAThr formation causes protein mistranslation
-
metabolism
-
in certain yeast mitochondria, CUN codons are reassigned from leucine to threonine, which requires an unusual tRNAThr with an enlarged 8-nt anticodon loop, tRNAThr1
metabolism
-
in certain yeast mitochondria, CUN codons are reassigned from leucine to threonine, which requires an unusual tRNAThr with an enlarged 8-nt anticodon loop, tRNAThr1. But in Candida albicans, the CUN codons remain assigned to leucine, and MST1 cannot threonylate tRNAThr
metabolism
in Arabidopsis thaliana, 18 aminoacyl-tRNA synthetases, aaRSs, including of AtThr-tRNA synthetase, are dually targeted to mitochondria and chloroplasts
physiological function
ApThrRS-1 catalyses only the aminoacylation of the cognate tRNA
physiological function
ApThrRS-2 is necessary for trans-editing, like the deaminoacylation of a misacylated serine moiety at the CCA terminus
physiological function
-
the final localisation of Thr-tRNA synthetase, expressed as a precursor protein, depends on the dual targeting peptide ThrRS-dTP
physiological function
-
amino acid discrimination does not occur at the aminoacyl transfer step. pre-Transfer hydrolysis contributes to proofreading only when the rate of transfer is slowed significantly. Thus, the relative contributions of pre- and posttransfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer
physiological function
a conserved, noncanonical function of tars regulates vascular development presumably by modulating the expression of vascular endothelial growth factor A (vegfa). Vegf signaling stimulates endothelial cell migration and proliferation by activating Vegf receptor tyrosine kinases
physiological function
-
aminoacyl-tRNA synthetases (aaRSs) catalyze the activation of the corresponding amino acids and attachment to their cognate tRNAs with extremely high fidelity due to pre- and post-transfer editing processes
physiological function
aminoacyl-tRNA synthetases maintain the fidelity during protein synthesis by selective activation of cognate amino acids at the aminoacylation site and hydrolysis of misformed aminoacyl-tRNAs at the editing site, crystal structure PDB ID 1TJE
physiological function
correct aminoacyl-tRNA generation is critical for the faithful transduction of genetic information, which is supported by the high levels of amino acid conservation in editing active sites of specific aaRSs across the three domains of life. Enzyme EcThrRS is an editing-capable enzyme, that can remove noncognate Ser. The N1 domain is essential for editing by EcThrRS. The enzyme shows strong tRNA-dependent editing, including the pre- and post-transfer editing of EcThrRS
physiological function
-
correct aminoacyl-tRNA generation is critical for the faithful transduction of genetic information, which is supported by the high levels of amino acid conservation in editing active sites of specific aaRSs across the three domains of life. The enzyme misactivates noncognate Ser and therefore requires an editing function to ensure the correct Thr-tRNAThr formation. Enzyme McThrRS is not able to hydrolyze Ser-tRNAThr and remove noncognate Ser. The degeneration of the crucial editing active sites of McThrRS impairs its posttransfer editing, McThrRS has lost its post-transfer editing activity, probably because of its degenerate editing active site in the N2 domain. McThrRS is unable to complement the loss of Saccharomyces cerevisiae thrS in vivo, because of its lack of editing activity
physiological function
Mesomycoplasma mobile
correct aminoacyl-tRNA generation is critical for the faithful transduction of genetic information, which is supported by the high levels of amino acid conservation in editing active sites of specific aaRSs across the three domains of life. The enzyme misactivates noncognate Ser and therefore requires an editing function to ensure the correct Thr-tRNAThr formation. Enzyme MmThrRS is able to hydrolyze Ser-tRNAThr and remove noncognate Ser. MmThrRS, which has an intact N2 domain, has post-transfer editing activity, editing-crucial residues include Lys86, Asp117, Cys119, and His123. MmThrRS has negligible tRNA-dependent pretransfer editing capacities. MmThrRS can complement the loss of Saccharomyces cerevisiae thrS in vivo, because of its lack of editing activity. The absence of the N1 domain of MmThrRS increases in vivo activity and optimizes enzyme protein structure/stability
physiological function
despite the absence of the editing domain, Saccharomyces cerevisiae mitochondrial ThrRS (ScmtThrRS) harbors a tRNA-dependent pretransfer editing activity. Only the usual tRNAThr2 stimulates pre-transfer editing, establishing the an example of a synthetase exhibiting tRNA-isoacceptor specificity during pre-transfer editing. The failure of tRNAThr1 to stimulate tRNA-dependent pre-transfer editing is due to the lack of an editing domain. tRNA-dependent pretransfer editing takes place in the aminoacylation catalytic core, tRNA-dependent editing process mechanism, overview. The anticodon nucleotides of SctRNAThr or tRNAThr2 are critical for the pre-transfer editing activity of SccytThrRS or ScmtThrRS
physiological function
interaction of the dual targeting peptide of Thr-tRNA synthetase with the chloroplastic receptor Toc34 (AtToc34) in Arabidopsis thaliana, analysis of mode of interactions of a dual targeting peptide with both Tom20 and Toc34. Effect of peptides corresponding to different segments of AtThrRS-dTP on in vitro import of organelle specific proteins. The N-terminal A2-Y29 segment of AtThrRS-dTP is essential for import into both organelles, while the C-terminal L30-P60 part is important for chloroplastic import efficiency. The recognition of the dual targeting peptide of AtThr-tRNA synthetase is different for the mitochondrial and chloroplastic receptors
physiological function
threonyl-tRNA synthetase (TARS) has an extracellular angiogenic activity separate from its function in protein synthesis. Strong association between the tumor expression of TARS and advancing stage of epithelial ovarian cancer, TARS expression and localization are also correlated with vascular endothelial growth factor (VEGF). Enzyme TARS is a regulator of the tumor microenvironment. TARS is secreted from ovarian cancer cells in response to cell stress
physiological function
threonyl-tRNA synthetase is essential for plant development by stabilizing of nuclear-encoded RNA polymerase (NEP) and plastid-encoded RNA polymerase (PEP) gene expressions and chloroplast protein synthesis. LAS is also essential for protein synthesis and construction of the ribosome system in rice chloroplasts
physiological function
-
despite the absence of the editing domain, Saccharomyces cerevisiae mitochondrial ThrRS (ScmtThrRS) harbors a tRNA-dependent pretransfer editing activity. Only the usual tRNAThr2 stimulates pre-transfer editing, establishing the an example of a synthetase exhibiting tRNA-isoacceptor specificity during pre-transfer editing. The failure of tRNAThr1 to stimulate tRNA-dependent pre-transfer editing is due to the lack of an editing domain. tRNA-dependent pretransfer editing takes place in the aminoacylation catalytic core, tRNA-dependent editing process mechanism, overview. The anticodon nucleotides of SctRNAThr or tRNAThr2 are critical for the pre-transfer editing activity of SccytThrRS or ScmtThrRS
-
physiological function
Mesomycoplasma mobile ATCC 43663
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correct aminoacyl-tRNA generation is critical for the faithful transduction of genetic information, which is supported by the high levels of amino acid conservation in editing active sites of specific aaRSs across the three domains of life. The enzyme misactivates noncognate Ser and therefore requires an editing function to ensure the correct Thr-tRNAThr formation. Enzyme MmThrRS is able to hydrolyze Ser-tRNAThr and remove noncognate Ser. MmThrRS, which has an intact N2 domain, has post-transfer editing activity, editing-crucial residues include Lys86, Asp117, Cys119, and His123. MmThrRS has negligible tRNA-dependent pretransfer editing capacities. MmThrRS can complement the loss of Saccharomyces cerevisiae thrS in vivo, because of its lack of editing activity. The absence of the N1 domain of MmThrRS increases in vivo activity and optimizes enzyme protein structure/stability
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additional information
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analysis of pre-transfer editing mechanism in yeast mitochondrial threonyl-tRNA synthetase (MST1) via the combined application of classical molecular dynamics and QM/MM-MD free energy calculations. The X-ray crystal structure of a single monomer of MST1 from Saccharomyces cerevisiae, PDB ID 3UH0 at 2.0 A resolution, is used as the starting structure for the computational studies. Molecular dynamics simulations, overview. Residues Gln180 and Gln292 are important in cofactor binding, Gln180 and Gln292 do not alternate in their H bonding to the Ser-AMP phosphate. Water molecules are able to enter and replace the H bonding networks and, as a result, MST1-bound Ser-AMP has increased variability in its positioning within the active site in comparison to Thr-AMP. A H-bond is intermittently formed between the alpha-amino group of the Thr and Ser and the side chain hydroxyl of Tyr270, though with markedly greater occurrence for Thr-AMP (22%) in comparison to Ser-AMP (7%). Mechanism of Thr-AMP and Ser-AMP hydrolysis determination by umbrella sampling on both ligands from three different initial conformations
additional information
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BaThrRS enzyme structure homology modeling based on the EThrRS structure from Escherichia coli, PDB ID 1QF6, optimization using molecular dynamics simulations, overview. The substrate-binding region in BaThrRS consists of Arg372, Glu374, Phe388, Gln493, Ser531, and Arg534, which correspond to residues Arg363, Glu365, Phe379, Gln479, Ser517, and Arg520 in EThrRS
additional information
molecular dynamics simulation study of the dynamics of the active site organization during charging step of dimeric ThrRS from Escherichia coli (ecThrRS) bound with ectRNAThr. The active site residues of the motif 2 loop approach the proximal bases of tRNA and adenylate by slow diffusive motion (in nanosecond time scale) and make conformational changes of the respective side chains via ultrafast librational motion to develop precise hydrogen bond geometry. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme. The presence of dynamically rigid zinc ion coordination sphere and bipartite mode of recognition of ectRNAThr are observed. Molecular dynamic simulation, overview
additional information
structure analysis of EcThrRS, functional importance of the Asp46 in the N1 domain and the Tyr173 in the N2 domain
additional information
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structure analysis of EcThrRS, functional importance of the Asp46 in the N1 domain and the Tyr173 in the N2 domain
additional information
the enzyme catalyzing the aminoacylation of tRNAThr1 and tRNAThr2, mitochondrial ThrRS (ScmtThrRS), encoded by the MST1 gene, is devoid of an editing domain, and consists only of the aminoacylation catalytic core connected to the C-terminal tRNA binding domain (CTD)
additional information
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the enzyme catalyzing the aminoacylation of tRNAThr1 and tRNAThr2, mitochondrial ThrRS (ScmtThrRS), encoded by the MST1 gene, is devoid of an editing domain, and consists only of the aminoacylation catalytic core connected to the C-terminal tRNA binding domain (CTD)
additional information
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the enzyme catalyzing the aminoacylation of tRNAThr1 and tRNAThr2, mitochondrial ThrRS (ScmtThrRS), encoded by the MST1 gene, is devoid of an editing domain, and consists only of the aminoacylation catalytic core connected to the C-terminal tRNA binding domain (CTD)
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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
E258K
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modified interation with the superrepressor, no activity
E259K
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modified interation with the superrepressor, unaltered activity
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/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
R583H
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modified interation of anticodon loop/C-ter domain, no activity
R609A
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modified interation of anticodon loop/C-ter domain, 35fold 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
K121A
no expression for the alanine mutant
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
Q362A
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the mutant displays increased Km values for tRNAThr2
R434A
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the mutant shows weaker binding for tRNAThr1 only
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
T357A
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the mutant displays increased Km values for tRNAThr2
Y405A
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the mutant displays increased Km values for tRNAThr2
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
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borrelidin-resistant derivative cell line 2000A
additional information
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borrelidin-resistant mutant
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
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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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Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.
Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes
Biochemistry
22
1934-1941
1983
Bos taurus
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Arbeeny, C.M.; Briden, K.L.; Stirewalt, W.S.
The activity and sedimentation properties of the aminoacyl-tRNA synthetases of rat skeletal muscle
Biochim. Biophys. Acta
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1979
Rattus norvegicus
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Freist, W.; Sternbach, H.; von der Haar, F.; Cramer, F.
Threonyl-tRNA, lysyl-tRNA and arginyl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogues
Eur. J. Biochem.
84
499-502
1978
Saccharomyces cerevisiae
brenda
Freist, W.; Gauss, D.H.
Threonyl-tRNA synthetase.
Biol. Chem. Hoppe-Seyler
376
213-224
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Aesculus hippocastanum, Geobacillus stearothermophilus, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Escherichia coli, Thermus thermophilus, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces pastorianus
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Ogata, K.; Kurahashi, A.; Nishiyama, C.; Terao, K.
Presence and role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol
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Rattus norvegicus
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Threonyl-tRNA synthetase from Thermus thermophilus. Purification and some structural and kinetic properties
Biochimie
76
71-77
1994
Escherichia coli, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Cura, V.; Kern, D.; Mitschler, A.; Moras, D.
Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data
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Thermus thermophilus
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Freist, W.; Sternbach, H.; Cramer, F.
Threonyl-tRNA synthetase from yeast. Discrimination of 19 amino acids in aminoacylation of tRNAThr-C-C-A and tRNAThr-C-C-A(2'NH2)
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745-752
1994
Saccharomyces cerevisiae
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Homo sapiens
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Crystals of threonyl-tRNA synthetase from Thermus thermophilus
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Thermus thermophilus
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Nameki, N.
Identity elements of tRNAThr towards Saccharomyces cerevisiae threonyl-tRNA synthetase
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Saccharomyces cerevisiae
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Aoyama, H.
Spermine stimulates the threonyl-tRNA formation in rat liver
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1990
Rattus norvegicus
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Holley, R.W.; Brunngraber, E.F.; Saad, F.; Williams, H.H.
Partial purification of the threonine- and tyrosine-activating enzymes from rat liver, and the effect of potassium ion on the activity of the tyrosine enzyme
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1961
Rattus norvegicus
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Effect of spermine on the reaction catalyzed by threonyl-tRNA synthetase from rat liver
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Rattus norvegicus
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Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12
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Escherichia coli
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Threonyl-transfer ribonucleic acid synthetase from Escherichia coli. Subunit structure and genetic analysis of the structural gene by means of a mutated enzyme and of a specialized transducing lambda bacteriophage
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1977
Escherichia coli, Escherichia coli overproducing
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Rapid purification of threonyl-tRNA synthetase from Saccharomyces carlsbergensis by affinity elution from phosphocellulose
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Saccharomyces pastorianus
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Purification and structural characterization of rat liver threonyl transfer ribonucleic acid synthetase
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4978-4984
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Rattus norvegicus
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Gerken, S.C.; Arfin, S.M.
Threonyl-tRNA synthetase from Chinese hamster ovary cells is phosphorylated on serine
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259
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Cricetulus griseus
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Cloning and characterization of the gene for the yeast cytoplasmic threonyl-tRNA synthetase
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6171-6183
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Saccharomyces cerevisiae, Saccharomyces cerevisiae D273-10B
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Interaction of eukaryotic threonyl-tRNA synthetase with high-Mr RNAs and tRNAThr
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169
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Oryctolagus cuniculus
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Bovee, M.L.; Pierce, M.A.; Francklyn, C.S.
Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase
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42
15102-15113
2003
Escherichia coli
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Dock-Bregeon, A.; Sankaranarayanan, R.; Romby, P.; Caillet, J.; Springer, M.; Rees, B.; Francklyn, C.S.; Ehresmann, C.; Moras, D.
Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem
Cell
103
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2000
Escherichia coli
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The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
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97
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1999
Escherichia coli
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Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex
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275
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Cricetulus griseus, Oryctolagus cuniculus
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Torres-Larios, A.; Sankaranarayanan, R.; Rees, B.; Dock-Bregeon, A.C.; Moras, D.
Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase
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Staphylococcus aureus (Q8NW68), Staphylococcus aureus
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The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression
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Escherichia coli
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Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase
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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase
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2002
Escherichia coli (P0A8M3), Escherichia coli
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Evolution and tRNA recognition of threonyl-tRNA synthetase from an extreme thermophilic archaeon, Aeropyrum pernix K1
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31
62-70
2003
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-
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