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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
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
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, low activity
-
-
?
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
-
-
-
-
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
-
-
-
?
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
-
-
?
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
-
reaction of EC 6.1.1.11, mischarging of tRNAThr
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
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, low activity
-
-
?
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
-
-
-
-
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
-
-
-
?
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
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
kinetics of the enzyme for cognate Thr and noncognate Ser are determined with an ATP-phosphate exchange reaction
-
additional information
additional information
-
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

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
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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