HOME
login
history
all enzymes
BRENDA home
History
Information on EC 6.1.1.3 - threonine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.1.1.3 threonine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.3
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodon
-
threonylation
- borrelidin
-
aarss
-
isoacceptors
- phenylalanyl-trna
-
noncognate
- alanyl-trna
-
post-transfer
- hisrs
- glyrs
-
mischarged
-
anticodon-like
-
misactivates
- seryl-trna
-
histidyl-trna
- lysyl-trna
-
anticodon-binding
-
pre-transfer
- asprs
-
trna-like
-
trna-dependent
- diagnostics
- drug development
The enzyme appears in viruses and cellular organisms
Synonyms
ApThrRS-1, ApThrRS-2, BaThrRS, EcThrRS, ectRNAThr, McThrRS, mitochondrial threonyl-tRNA synthetase, MJ1197, MmThrRS, More, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ApThrRS-1
ApThrRS-2
mitochondrial threonyl-tRNA synthetase
MJ1197
MmThrRS
Mst1
ScmtThrRS
Synthetase, threonyl-transfer ribonucleate
TarS
Thr-tRNA synthetase
Threonine translase
Threonine--tRNA ligase
Threonine-transfer ribonucleate synthetase
Threonyl-ribonucleic synthetase
Threonyl-transfer ribonucleate synthetase
Threonyl-transfer ribonucleic acid synthetase
Threonyl-transfer RNA synthetase
Threonyl-tRNA synthetase
ThrRS
ThrS
TRS
additional information
-
the enzyme belongs to the class II aminoacyl-tRNA synthetases
Synthetase, threonyl-transfer ribonucleate
-
-
-
-
Synthetase, threonyl-transfer ribonucleate
-
-
Threonine translase
-
-
-
-
Threonine--tRNA ligase
-
-
-
-
Threonine-transfer ribonucleate synthetase
-
-
-
-
Threonine-transfer ribonucleate synthetase
-
-
Threonyl-ribonucleic synthetase
-
-
-
-
Threonyl-transfer ribonucleate synthetase
-
-
-
-
Threonyl-transfer ribonucleate synthetase
-
-
Threonyl-transfer ribonucleic acid synthetase
-
-
-
-
Threonyl-transfer ribonucleic acid synthetase
-
-
Threonyl-transfer RNA synthetase
-
-
-
-
Threonyl-transfer RNA synthetase
-
-
Threonyl-tRNA synthetase
-
-
-
-
Threonyl-tRNA synthetase
-
-
ThrRS
-
-
-
-
ThrRS
-
-
TRS
-
-
-
-
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 SOURCE
PATHWAYS
BRENDA
MetaCyc
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.
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.
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
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
MST1 can attach threonine to both tRNAThr1 and the regular tRNAThr2, but not to the wild-type tRNAHis. But a loss of the first nucleotide G-1 in tRNAHis converts it to a substrate for MST1
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
substrate binding induces conformational changes
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
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
?
-
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
-
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
-
additional information
?
-
-
structure-based evolutionary considerations
-
-
-
additional information
?
-
-
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
?
-
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
-
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
-
additional information
?
-
proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. A unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes
-
-
-
additional information
?
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
-
additional information
?
-
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
-
additional information
?
-
L-serine is a poor substrate for the wild-type enzyme, the N-terminal enzyme domain is responsible for editing
-
-
-
additional information
?
-
-
L-serine is a poor substrate for the wild-type enzyme, the N-terminal enzyme domain is responsible for editing
-
-
-
additional information
?
-
-
the enzyme examines side chain structures of amino acids in 4 recognition steps. For each step the enzyme uses special distinct structures or conformations of the binding cleft
-
-
-
additional information
?
-
-
specificity with regard to amino acids, discrimination factors
-
-
-
additional information
?
-
-
addition of first nucleotide G-1 to tRNAThr1 allows efficient histidylation by histidyl-tRNA synthetase
-
-
-
additional information
?
-
-
no activity with L-Val, L-Ala, or L-Cys
-
-
-
additional information
?
-
ScmtThrRS exhibits a tRNA-dependent pre-transfer editing activity that is specific for the tRNAThr2 isoacceptor, whereas tRNAThr1 is unable to stimulate such activity. Editing capability of tRNAThr1 with requirement for the presence of an editing domain
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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 + 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
-
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q980D1
-
-
-
r
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
-
-
-
-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
Q8NW68
-
-
?
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
?
-
Q980D1
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
-
additional information
?
-
-
a freestanding proofreading domain is required for protein synthesis quality control in archaea
-
-
-
additional information
?
-
-
no activity with L-Val, L-Ala, or L-Cys
-
-
-
additional information
?
-
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
-
-
-
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.
INHIBITOR
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.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthritis
Dermatomyositis with erosive arthropathy: association with the anti-PL-7 antibody.
Brucellosis, Bovine
Exploring the Molecular Basis for Binding of Inhibitors by Threonyl-tRNA Synthetase from Brucella abortus: A Virtual Screening Study.
Dermatomyositis
Dermatomyositis with erosive arthropathy: association with the anti-PL-7 antibody.
Dermatomyositis
Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells.
Dermatomyositis
Polydermatomyositis with anti-PL7 antibody: clinical and laboratory follow-up over a five year period.
Joint Diseases
Dermatomyositis with erosive arthropathy: association with the anti-PL-7 antibody.
Leishmaniasis, Visceral
Genetic manipulation of Leishmania donovani threonyl tRNA synthetase facilitates its exploration as a potential therapeutic target.
Mitochondrial Diseases
A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional Defects.
Mitochondrial Encephalomyopathies
A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional Defects.
Myositis
Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase.
Myositis
Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis.
Neoplasms
Assessing the effects of threonyl-tRNA synthetase on angiogenesis-related responses.
Ovarian Neoplasms
Threonyl-tRNA synthetase overexpression correlates with angiogenic markers and progression of human ovarian cancer.
Pancreatic Neoplasms
Inhibition of MUC1 biosynthesis via threonyl-tRNA synthetase suppresses pancreatic cancer cell migration.
Polymyositis
Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells.
Polymyositis
Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase.
Polymyositis
Onset of polymyositis with autoantibodies to threonyl-tRNA synthetase during pregnancy.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Borrelidin, a small molecule nitrile-containing macrolide inhibitor of threonyl-tRNA synthetase, is a potent inducer of apoptosis in acute lymphoblastic leukemia.
Starvation
Aminoacyl-tRNA synthetase gene regulation in Bacillus subtilis: induction, repression and growth-rate regulation.
Starvation
Processing of the leader mRNA plays a major role in the induction of thrS expression following threonine starvation in Bacillus subtilis.
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
0.11
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
-
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
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
13.5
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
60
65
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
-
-
brenda