HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 6.1.1.3 - threonine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.3
Word Map on EC 6.1.1.3
- 6.1.1.3
-
synthetases
- aminoacyl-trna
-
aminoacylation
-
anticodon
-
threonylation
-
aarss
- borrelidin
-
isoacceptors
- phenylalanyl-trna
-
noncognate
- glyrs
-
post-transfer
- alanyl-trna
-
mischarged
- hisrs
-
misactivates
-
anticodon-like
-
pre-transfer
-
lysyl-trna
-
anticodon-binding
- serrs
-
trna-dependent
- asprs
-
trna-like
-
seryl-trna
-
histidyl-trna
- diagnostics
- drug development
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
6.1.1.3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
threonine-tRNA ligase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
; bi uni uni bi ping-pong mechanism
-
-
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
induced fit, Trp434 is involved in conformational changes during substrate binding
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
functional mechanism and substrate recognition, editing model, 2 separate active sites for substrate binding, binding of tRNA is more specific than the binding of the amino acid
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
mechanism, active site structure, and substrate recognition method
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
substrate binding and mechanism
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
the catalytic domain is located at the C-terminus of the enzyme
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
active site structure
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
determination of substrate binding sites, catalytic sites, and catalytic mechanism from structure modeling
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
reaction mechanism analysis by QM/MM and MM modeling of full length and truncated enzyme, molecular mechanism simulation
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
reaction mechanism and structure-function relationship, modeling, overview
-
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
reaction mechanism and structure-function relationship, overview. 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-threonine:tRNAThr ligase (AMP-forming)
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9023-46-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS
-
-
several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS
-
-
-
Uniprot
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
sequence comparison of threonyl-tRNA synthetases from Brucella abortus (BaThrRS) and Escherichia coli (EThrRS), which reveals 51% sequence identity
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
-
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
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
-
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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
-
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
-
threonyl-tRNA synthetase overexpression correlates with angiogenic markers and progression of human ovarian cancer
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
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
-
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. But in Candida albicans, the CUN codons remain assigned to leucine, and MST1 cannot threonylate tRNAThr
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 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; 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
-
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
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
-
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
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
-
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
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
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
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
-
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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
-
additional information
-
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
-
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
-
structure analysis of EcThrRS, functional importance of the Asp46 in the N1 domain and the Tyr173 in the N2 domain
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
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-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-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 + 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
-
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
-
-
-
-
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
-
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
-
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
-
-
-
-
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
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
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
-
-
-
-
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
-
-
-
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
Saccharomyces cerevisiae ATCC 204508 / S288c
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
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
?
-
-
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
?
-
-
structure-based evolutionary considerations
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Saccharomyces cerevisiae ATCC 204508 / S288c
ScmtThrRS exhibits a tRNA-dependent pre-transfer editing activity that is specific for the tRNAThr2 isoacceptor, whereas tRNAThr1 is unable to stimulate such activity. Editing capability of tRNAThr1 with requirement for the presence of an editing domain
-
-
-
additional information
?
-
Saccharomyces cerevisiae ATCC 204508 / S288c
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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-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
Q6KH76
reaction of EC 6.1.1.11, mischarging of tRNAThr, low activity
-
-
?
ATP + L-serine + tRNAThr
AMP + diphosphate + L-seryl-tRNAThr
Q6KH76
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
Q9YDW0, Q9YFY3
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q9YDW0, Q9YFY3
-
-
-
?
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
F4IFC5
-
-
-
?
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
P0A8M3
-
-
?
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
P0A8M3
-
-
-
?
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
P26639
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q58597
-
-
-
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
Q6KH76
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q6KH76
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q9UZ14
-
-
-
?
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
Q8NW68
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q980D1
-
-
-
r
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
P07236
-
-
-
?
ATP + L-threonine + tRNAThr1
AMP + diphosphate + L-threonyl-tRNAThr1
Saccharomyces cerevisiae ATCC 204508 / S288c
P07236
-
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
P07236
-
-
-
?
ATP + L-threonine + tRNAThr2
AMP + diphosphate + L-threonyl-tRNAThr2
Saccharomyces cerevisiae ATCC 204508 / S288c
P07236
-
-
-
?
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
?
-
F4IFC5
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
?
-
Q58597
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
?
-
-
no activity with L-Val, L-Ala, or L-Cys
-
-
-
additional information
?
-
P07236
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
?
-
Saccharomyces cerevisiae ATCC 204508 / S288c
P07236
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
?
-
Q980D1
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
identification of the ATP-binding regions of BaThrRS, docking of ATP to the protein, and modeling of the binding structure, predicted binding mode of ATP, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Ni2+
the enzyme can bind one Ni2+ per subunit, binding of nickel inhibits the oxidation of enzyme residue Cys182 by H2O2 or air
Phosphorus
-
phosphoprotein containing phosphoserine, activity can be modulated by reversible phosphorylation
Zn2+
Mg2+
-
Mg2+ can be substituted by Ca2+ and Mn2+. Zn2+ and Ni2+ can only very poorly replace Mg2+; required
Zn2+
-
used to discriminate against the isosteric valine at the activation step
Zn2+
-
mediates amino acid discrimination of the enzyme, located in the active site, formation of a pentacoordinate intermediatewith both the amino group and the side chain hydroxyl of L-threonine
Zn2+
-
the presence of dynamically rigid zinc ion coordination sphere and bipartite mode of recognition of ectRNAThr are observed
Zn2+
the enzyme can bind one Zn2+ per subunit, crystal structure analysis, PDB ID 1EVK, residues C334, H385 and H511 coordinate a zinc ion, which is essential for aminoacylation. Binding of zinc inhibits the oxidation of enzyme residue Cys182 by H2O2 or air
Zn2+
-
zinc binding in the catalytic site, the active site zinc atom is essential for the recognition of threonine, three amino acids forming the zinc-binding site, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3R)-2-amino-N-(((E)-3-(6-aminopyrimidin-4-yl)styryl)-sulfonyl)-3-hydroxy-4-methylpentanamide
(2S,3R)-2-amino-N-((3-(1-amino-3-chloroisoquinolin-6-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-((7-(6-aminopyrimidin-4-yl)naphthalen-2-yl)sulfonyl)-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
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
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
ZINC27215482
-
docking analysis, overview. The best inhibitor, which can be used to develop novel drugs against bovine brucellosis
(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-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
-
-
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
-
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
3-hydroxynorvaline enhances the ATPase function of the synthetic site, at a rate not increased by nonaminoacylatable tRNA
-
spermine
-
has a stimulatory and synergistic effect with Mg2+, cannot replace Mg2+ in activation
spermine
-
no effect on the overall reaction as well as on the rate of ATP-diphosphate exchange. At low Mg2+ (1 mM) concentration spermine activates 8fold ATP-diphosphate exchange and 23fold the threonyl-tRNA synthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
120
L-serine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
0.1
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
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
0.00013
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; 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; 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; 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; 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
-
0.000037 - 0.00007
tRNAThr
-
of Thermus thermophilus, , depending on temperature
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
-
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
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
-
pre-steady-state kinetics, kinetics of ATPase activity in presence of 3-hydroxynorvaline, overview
-
additional information
additional information
-
kinetics of MST1 with different tRNAs, overview
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.9
L-threonine
pH 7.2, 60°C, recombinant 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
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; mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication; mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication; 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; 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
-
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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
L-serine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
11.18
L-threonine
-
in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002262 - 0.05
(2S,3R)-2,3-diamino-N-(((E)-3-(6-aminopyrimidin-4-yl)-styryl)sulfonyl)butanamide
0.0000039 - 0.000091
(2S,3R)-2-amino-3-hydroxy-N-((3-(1-oxoisoindolin-5-yl)-phenyl)sulfonyl)butanamide
0.000083 - 0.00582
(2S,3R)-2-amino-3-hydroxy-N-((3-(3-methyl-1H-indazol-5-yl)phenyl)sulfonyl)butanamide
0.05
(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
0.000004 - 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
0.000132 - 0.05
tert-butyl((2S,3R)-1-(3-(1H-indazol-5-yl)-benzenesulfonamido)-3-(tert-butoxy)-1-oxobutan-2-yl)-carbamate
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
0.000132
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
7.7