Information on EC 6.1.1.10 - methionine-tRNA ligase

New: Word Map on EC 6.1.1.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
6.1.1.10
-
RECOMMENDED NAME
GeneOntology No.
methionine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
active site structure and reaction mechanism involving Tyr15 and Thr10, Tyr94 is involved in maintaining the native enzyme conformation
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
amino acid residues D138, R139, and F135 are important for activity
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
amino acid residues involved in tRNA binding are K30, N66, S78, and M81
Q9V011
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
mechanism, catalytic domain is formed by amino acid residues A215-K823
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
reaction mechanism, Lys261, Lys295, and Lys301 are located in the catalytic crevice of the enzyme
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
substrate binding and mechanism
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
substrate recognition and structure
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
substrate recognition, editing, binding and reaction mechanism
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
the amino acid acceptor arm of tRNAMet binds to the plant enzyme
Q9ZTS1
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
the anticodon sequence is important for tRNA substrate specificty
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
two-step reaction process via anenzyme-L-Met-AMP intermediate
P56192
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
the aminoacylation reaction is a two-step mechanism: in the first step, the synthetase recognizes the appropriate amino acid and activates it with ATP to form the activated intermediate, an aminoacyl-adenylate, aa-AMP, the second step transfers the aminoacyl moiety onto the 3'-hydroxyl of the CCA end of the tRNA, the methionine-binding pocket is composed of residues Ala12, Leu13, Tyr15, Trp253, Ala256, Pro257, Tyr260, Ile297, His301, and Trp305
-
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
the anticodon sequence is important for tRNA substrate specificty
Haloferax volcanii WFD11
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
-
-
-
-
esterification
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
methionine metabolism
-
-
Selenocompound metabolism
-
-
tRNA charging
-
-
SYSTEMATIC NAME
IUBMB Comments
L-methionine:tRNAMet ligase (AMP-forming)
In those organisms producing N-formylmethionyl-tRNAfMet for translation initiation, this enzyme also recognizes the initiator tRNAfMet and catalyses the formation of L-methionyl-tRNAfMet, the substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Methionine translase
-
-
-
-
Methionine--tRNA ligase
-
-
-
-
Methionyl tRNA synthetase
-
-
-
-
Methionyl-transfer ribonucleate synthetase
-
-
-
-
Methionyl-transfer ribonucleic acid synthetase
-
-
-
-
Methionyl-transfer RNA synthetase
-
-
-
-
MetRS
-
-
-
-
Synthetase, methionyl-transfer ribonucleate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-22-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a single gene of chloroplast origin codes for mitochondrial and chloroplastic isozyme
-
-
Manually annotated by BRENDA team
a single gene of chloroplast origin codes for mitochondrial and chloroplastic isozyme
SwissProt
Manually annotated by BRENDA team
UM23C1-1and GRI strains, genes metS1 and metS2
-
-
Manually annotated by BRENDA team
class I enzyme
SwissProt
Manually annotated by BRENDA team
class I enzyme
-
-
Manually annotated by BRENDA team
gene metE
-
-
Manually annotated by BRENDA team
M547 and mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant
-
-
Manually annotated by BRENDA team
purified recombinant C-terminally truncated enzyme
-
-
Manually annotated by BRENDA team
strain EM
-
-
Manually annotated by BRENDA team
strain K12, and mutant strains with an increased Km for methionine
-
-
Manually annotated by BRENDA team
wild-type enzyme and mutants produced by site-directed mutagenesis
-
-
Manually annotated by BRENDA team
Escherichia coli EM
strain EM
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12, and mutant strains with an increased Km for methionine
-
-
Manually annotated by BRENDA team
MS534, purified recombinant dimeric wild-type and monomeric truncated mutant enzymes expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
strain WFD11
-
-
Manually annotated by BRENDA team
Haloferax volcanii WFD11
strain WFD11
-
-
Manually annotated by BRENDA team
class I enzyme
Uniprot
Manually annotated by BRENDA team
Lupinus sp.
yellow lupin
-
-
Manually annotated by BRENDA team
non-typical class I enzyme lacking the Zn2+ binding motif and the C-terminal dimerization appendix which is found in enzymes from other organisms
-
-
Manually annotated by BRENDA team
enzyme contains a supplementary C-terminal domain related to endothelial monocyte activating polypeptide II, i.e. EMAPII, a cytokine
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 8944
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans 8944
strain 8944
-
-
Manually annotated by BRENDA team
class I enzyme
Uniprot
Manually annotated by BRENDA team
2 cytoplasmic and mitochondrial isozymes
-
-
Manually annotated by BRENDA team
a strain carrying the MES1 structure gene on a high copy number plasmid (pFL1)
-
-
Manually annotated by BRENDA team
class I enzyme
-
-
Manually annotated by BRENDA team
strain HB8, class Ia enzyme
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
MetRS from nematode is functionally related to human MetRS despite the fact that their appended tRNA-binding domains have distinct structural folds, and are not orthologues
physiological function
-
the enzyme also provides a cytosolic anchoring site for aminoacyl-tRNA synthetase-interacting multifunctional protein-3 (AIMP3)/p18, a potent tumor suppressor that is translocated to the nucleus for DNA repair upon DNA damage which is released from the enzyme by UV irradiation-induced stress. The enzyme plays a role as a coregulator with eukaryotic initiation factor-2 subunit-alpha for general control nonrepressed-2-mediated translational inhibition and as a coupler of translational inhibition and DNA repair following DNA damage by releasing bound tumor suppressor AIMP3 for its nuclear translocation
metabolism
-
the single MetRS of Trypanosoma brucei is essential for normal cell growth
additional information
-
the catalytic domains of class I aminoacyl-tRNA synthetases are built around a conserved Rossmann nucleotide binding fold, with additional polypeptide domains responsible for tRNA binding or hydrolytic editing of misacylated substrates, structural comparisons of class Ia and Ib enzymes, overview. Structural integrity of the helix-turn-strand-helix motif contributes more to tRNA aminoacylation than does amino acid identity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (S)-2-aminohex-5-enoic acid + tRNAMet
AMP + diphosphate + (S)-2-aminohex-5-enoyl-tRNAMet
show the reaction diagram
-
1850fold reduced activity compared to L-methionine
-
?
ATP + (S)-2-aminohex-5-ynoic acid + tRNAMet
AMP + diphosphate + 2(S)-aminohex-5-ynoyl-tRNAMet
show the reaction diagram
-
500fold reduced activity compared to L-methionine
-
?
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucyl-tRNAMet
show the reaction diagram
-
activity of mutant L13G, overview
-
-
?
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucinyl-tRNAMet
show the reaction diagram
-
MetRS SLL-mutant
-
-
?
ATP + L-homocysteine + tRNAMet
?
show the reaction diagram
-
edition and aminoacylation by cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAArg(CCU)
?
show the reaction diagram
-
tRNA mismethionylation
-
-
?
ATP + L-methionine + tRNAAsp
AMP + diphosphate + L-methionyl-tRNAAsp
show the reaction diagram
Q9ZTS1
only the wild-type enzyme, not the C-terminally deleted enzyme mutant
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Lupinus sp.
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P00959
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P56192
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
O23761, Q91UL7
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
O74634
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9ZTS1
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P00958
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
A0R3E2
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q181D9
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P56192
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q38C91
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
substrates: prokaryotic, chloroplastic, cytoplasmic (initiator not non-initiator)
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
O74634
also utilizes both subtypes of Escherichia coli tRNAMet
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
also utilizes tRNAMet from Escherichia coli
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P00959
binding of L-methionine induces conformational changes of the active site of the enzyme, amino acid residues Y15 and W253 are important for the strength of binding, H301 is responsible for the specific recognition of the sulfur atom of methionine
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
covalent binding of methionine to the tRNAMet
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
dimerization of the enzyme is required for affinity to tRNAMet
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
formation of an methionine adenylate reaction intermediate
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
initiator and elongation tRNAMet, cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
reduced activity with L-methionine analogues, overview, two-step reaction, the first step, the aminoacylation, is reversible, the seconde, the transfer reaction, is not
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
substrate editing mechanism, L-methionine is bound to a hydrophobic pocket formed by amino acid residues W253, Y15, A256, P257, L13, A12, I297, Y260, H301, and W305 around the side-chain
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
the C-terminal ancillary RNA-binding domain is important for activity and has dual function provided by 2 structural motifs: 1. the helix-turn-helix HTH motif, which confers rate-limiting dissociation of the aminoaclyted tRNA from the enzyme, and 2. the KGKKKK lysine-rich cluster LRC, which is probably involved in accelerating the association step of deacylated tRNA
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9ZTS1
the EMAPII-like C-terminal appendix domain provides the enzyme with non-specific tRNA binding properties, the deleted enzyme form missing this domain is therefore more specific and shows a 10fold lower Km for the tRNA substrate, enzyme is also active with tRNAMet from Saccharomyces cerevisiae
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
two-step reaction mechanism, enzyme forms the reaction intermediate L-methionyl-adenylate, which covalently methionylates the enzyme at the epsilon-amino group of a lysine residue, inducing structural modifcation, 4.3 and 2.2 mol of Met are incorporated by 1 mol of wild-type enzyme and truncated mutant enzyme, respectively
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
L-methionine and methionine analogue substrates are incorporated in proteins, overview
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
protein biosynthesis in archaea is initiated with methionine not with formylmethionine
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
the nucleolar located enzyme is related to rRNA synthesis, the cytoplasmic enzyme is involved in protein biosynthesis
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P56192
human mitochondrial wild-type and mutant mtRNAs: T5048 deletion, and T5052C or T5012A point mutations, initiator tRNA from Escherichia coli, tRNAMet from Bos taurus
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
structural basis for anticodon recognition by the enzyme, catalytic Rossmann fold domain
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
tRNA anticodon binding site structure
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
essentiality of the metS1, nonessentiality of the metS2 for vegetative growth
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
the MetRS specificity for methionine and conformity with the identity rules for tRNAMet for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
conformation of tRNA and the recognition of anticodon by MetRS, hydrogen bonding patterns, interactions at the active site, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
functional idiosyncrasies of the viral MetRS, activity with Escherichia coli native tRNAMet and initiator tRNAMet, and Saccharomyces cerevisiae native tRNAMet and initiator tRNAMet, overview, the MetRS specificity for methionine and recognition of the tRNAMet acceptor stem show conformity with the identity rules for tRNAMet for archea/eukarya, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
residues L13, P257, Y260, and H301 are involved in the Met binding site
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
MetRS specifically binds tRNAMet and catalyzes the synthesis of methionyl-tRNAMet. The C-terminal appended domain causes a slow release of aminoacyl-tRNA and establishes a limiting step in the global aminoacylation reaction
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q181D9
active site analysis and docking study, overview. Key residues are His53, Asp51 and Lys56 consistently forming H-bonding interactions with the carboxylic acid moiety of methionine. Ile12 forms a hydrogen bond with this moiety in different dockings and the residues Ile224, Val226 and Ala230 form a hydrophobic pocket
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
analysis of methionine and adenosine binding to MetRS, catalytic domain structure, overview. The KMSKS domain, residues 293-350, or stem contact fold domain, with a beta-alpha-alpha-beta-alpha topology domain, connects the catalytic domain with the anticodon domain, KMSKS domain conformation and structure, modelling, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
binding structures of substrates and products, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Escherichia coli EM
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Haloferax volcanii WFD11
-
protein biosynthesis in archaea is initiated with methionine not with formylmethionine
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Escherichia coli K12
-
-
-
-
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Paracoccus denitrificans 8944
-
-
-
-
ATP + L-methionine + tRNAThr(CGU)
?
show the reaction diagram
-
tRNA mismethionylation
-
-
?
ATP + L-norleucine + tRNAMet
AMP + diphosphate + L-norleucyl-tRNAMet
show the reaction diagram
-
-
-
-
-
ATP + L-norleucine + tRNAMet
AMP + diphosphate + L-norleucyl-tRNAMet
show the reaction diagram
-
1050fold reduced activity compared to L-methionine
-
?
ATP + L-trans-alpha-crotylglycine + tRNAMet
AMP + diphosphate + L-trans-alpha-crotylglycyl-tRNAMet
show the reaction diagram
-
4700fold reduced activity compared to L-methionine
-
?
ATP + L-valine + tRNAMetG34C36
AMP + diphosphate + L-valyl-tRNAMetG34C36
show the reaction diagram
-
anticodon mutant initiator tRNAMet, reduced reverse, i.e. deacetylation, reaction, CAU to GAC anticodon mutant initiator tRNAMet, reduced reverse, i.e. deacetylation, reaction
-
r
ATP + L-valine + tRNAMetG34C36
AMP + diphosphate + L-valyl-tRNAMetG34C36
show the reaction diagram
Haloferax volcanii WFD11
-
anticodon mutant initiator tRNAMet, reduced reverse, i.e. deacetylation, reaction, CAU to GAC anticodon mutant initiator tRNAMet, reduced reverse, i.e. deacetylation, reaction
-
r
ATP + methionine + hydroxylamine
methionine hydroxamate + AMP + diphosphate
show the reaction diagram
Paracoccus denitrificans, Paracoccus denitrificans 8944
-
-
-
-
ATP + selenomethionine + tRNAMet
AMP + diphosphate + selenomethionyl-tRNAMet
show the reaction diagram
-
-
-
-
ATP + selenomethionine + tRNAMet
AMP + diphosphate + selenomethionyl-tRNAMet
show the reaction diagram
Paracoccus denitrificans, Paracoccus denitrificans 8944
-
-
-
-
-
CoA + L-methionine
Met-S-CoA
show the reaction diagram
-
-
-
?
additional information
?
-
-
also catalyzes selenomethionine- and selenoethionine-dependent ATP-diphosphate exchange, no other amino acid than methionine is activated in ATP-diphosphate exchange
-
-
-
additional information
?
-
-
no other amino acid than methionine is activated in ATP-diphosphate exchange
-
-
-
additional information
?
-
-
homocysteine thiolactone is formed as a product of an error-editing reaction, which prevents incorporation of homocysteine into tRNA and protein (not enzyme from temperature-sensitive mutant of CHO-cells, at non-permissive temperature)
-
-
-
additional information
?
-
-
enzyme forms A and B show differences in their capacity to recognize the cognate tRNAs
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
Lupinus sp.
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
29, 33, 34
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
methionine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
also catalyzes L-homocysteine, L-selenocysteine and norleucine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the isozymes also perform the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure
-
?
additional information
?
-
-
no activity with the CAU to CUA initiator tRNAMet mutant in vivo
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
P56192
the enzyme performs ATP/diphosphate exchange in absence of substrates
-
-
-
additional information
?
-
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
P00958
MetRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
-
-
-
additional information
?
-
-
modeling of the structure of a complex consisting of MetRS, tRNA, and activated methionine, molecular dynamics simulations, evaluation of the equilibrated structure of the complex and the cross-correlations between the residues in MetRS, analysis of communication between the activation site and the anticodon recognition site, overview
-
-
-
additional information
?
-
Q181D9
Met-tRNA anticodon interactions with the MetRS homology model, overview
-
-
-
additional information
?
-
Haloferax volcanii WFD11
-
no activity with the CAU to CUA initiator tRNAMet mutant in vivo
-
?
additional information
?
-
Paracoccus denitrificans 8944
-
methionine-dependent ATP-diphosphate exchange, also catalyzes L-homocysteine, L-selenocysteine and norleucine-dependent ATP-diphosphate exchange
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucyl-tRNAMet
show the reaction diagram
-
activity of mutant L13G, overview
-
-
?
ATP + L-homocysteine + tRNAMet
?
show the reaction diagram
-
edition and aminoacylation by cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P00959
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P56192
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9V011
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
O23761, Q91UL7
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
O74634
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q9ZTS1
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P00958
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
A0R3E2
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q181D9
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
P56192
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Q38C91
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
initiator and elongation tRNAMet, cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
L-methionine and methionine analogue substrates are incorporated in proteins, overview
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
protein biosynthesis in archaea is initiated with methionine not with formylmethionine
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
the nucleolar located enzyme is related to rRNA synthesis, the cytoplasmic enzyme is involved in protein biosynthesis
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
essentiality of the metS1, nonessentiality of the metS2 for vegetative growth
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
the MetRS specificity for methionine and conformity with the identity rules for tRNAMet for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
-
MetRS specifically binds tRNAMet and catalyzes the synthesis of methionyl-tRNAMet. The C-terminal appended domain causes a slow release of aminoacyl-tRNA and establishes a limiting step in the global aminoacylation reaction
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
Haloferax volcanii WFD11
-
protein biosynthesis in archaea is initiated with methionine not with formylmethionine
-
r
ATP + L-valine + tRNAMetG34C36
AMP + diphosphate + L-valyl-tRNAMetG34C36
show the reaction diagram
Haloferax volcanii, Haloferax volcanii WFD11
-
CAU to GAC anticodon mutant initiator tRNAMet, reduced reverse, i.e. deacetylation, reaction
-
r
additional information
?
-
-
L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure
-
?
additional information
?
-
-
no activity with the CAU to CUA initiator tRNAMet mutant in vivo
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
Haloferax volcanii WFD11
-
no activity with the CAU to CUA initiator tRNAMet mutant in vivo
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
supports methionine-dependent ATP-diphosphate exchange with 14% of the efficiency of Mg2+
Co2+
-
supports methionine-dependent ATP-diphosphate exchange with 20% of the efficiency of Mg2+
K+
-
in presence of 15 mM Mg2+, K+ stimulates up to concentration of about 50 mM, inhibits at higher concentrations. Unable to stimulate aminoacylation in absence of Mg2+
KCl
Q9V011
-
KCl
P56192
stimulates
Mg2+
-
2 (ATP-diphosphate exchange), 1.5 (aminoacylation)
Mg2+
-
absolutely dependent on; optimal concentration: 10 mM
Mg2+
-
2; absolutely dependent on
Mg2+
-
absolutely dependent on; optimal Mg2+/ATP ratio: 2.5
Mg2+
Q9V011
-
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required. The Mg2+ ion has six atoms arranged in a square bipyramidal coordination shell and bridges the diphosphate and MetAMP products. It is interacting with two oxygen atoms from two different phosphoryl groups of the diphosphate, one oxygen from the MetAMP phosphoryl group, and three water molecules, though one of these is a bit distant for a typical Mg2+ ligand at approximately 2.5 A
Mg2+
Q181D9
required
Mg2+
-
required
Mn2+
-
enzyme binds 2 Mn2+ per dimer, no binding with the trypsin-modified monomer
Mn2+
-
optimal Mn2+/ATP ratio: 1 (ATP-diphosphate exchange), 1.5 (aminoacylation)
NH4+
-
in presence of 15 mM Mg2+, NH4+ stimulates up to a concentration of about 50 mM, inhibits at higher concentrations. In presence of 0.5 mM Mg2+, NH4+ alone stimulates aminoacylation
Zn2+
-
2 tightly bound Zn2+ per polypeptide chain, in the vicinity of the active site
Zn2+
-
contains two zinc atoms per dimer, one per subunit
Zn2+
-
2 binding sites, 0.14 mM tightly bound zinc is present in 1 mol of cytoplasmic isozyme, but not in the mitochondrial one, required for stability and activity of the cytoplasmic isozyme
Zn2+
Q9V011
two Zn2+ per protomer, binding site structures
Zn2+
-
2 Zn2+ tightly bound per enzyme molecule
Zn2+
-
required
Zn2+
-
binding domain and binding structure, overview
Zn2+
Q181D9
zinc is an absolute requirement for enzyme activity, binding site residues, overview
Mn2+
-
supports methionine-dependent ATP-diphosphate exchange with 15% of the efficiency of Mg2+
additional information
-
enzyme lacks Zn2+ binding motif and contains no Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-amino-heptanoic acid
-
L-methionine analogue, competitive
(S)-2-aminohex-5-enoic acid
-
L-methionine analogue, competitive
(S)-2-aminohex-5-ynoic acid
-
L-methionine analogue, competitive
1,10-phenanthroline
-
little or no inhibition by 1,7-phenanthroline and 4,7-phenanthroline
1,10-phenanthroline
-
complete inhibition of the cytoplasmic isozyme at 1 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0035 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 40 nM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.099 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 170 nM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0066 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 340 nM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0035 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 18 nM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0013 mM
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 180 nM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.001 mM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 87 nM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0031 mM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 760 nM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 1670 nM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.099 mM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 170 nM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0059 mM
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 850 nM
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 70 nM
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-3-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-4-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 680 nM
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 510 nM
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-3-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-4-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 1100 nM
1-[2-(4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-piperidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
-
1-[3-[(3,5-dibromobenzyl)amino]propyl]-3-phenylurea
-
-
1-[3-[(3,5-dibromobenzyl)amino]propyl]-3-phenylurea
-
IC50 is 330 nM
1-[[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.027 mM
1-[[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 430 nM
1-[[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0061 mM
1-[[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 810 nM
2,2'-dipyridyl
-
-
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-4H-chromen-4-one
-
-
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-4H-chromen-4-one
-
IC50 is 0.001 mM
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
-
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
IC50 is below 0.3 nM
2-([3-[(2,3-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
77.9% inhibition at 50 nM
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 9.7 nM
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 4.9 nM
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(2,4-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
87.1% inhibition at 50 nM
2-([3-[(2,5-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
93.1% inhibition at 50 nM
2-([3-[(2,6-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
51.3% inhibition at 50 nM
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 7.0 nM
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 3.3 nM
2-([3-[(2-chlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
31.8% inhibition at 50 nM
2-([3-[(3,4-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
91.7% inhibition at 50 nM
2-([3-[(3,4-dichlorobenzyl)amino]propyl]thio)quinolin-4(1H)-one
-
-
2-([3-[(3,4-dichlorobenzyl)amino]propyl]thio)quinolin-4(1H)-one
-
IC50 is 680 nM
2-([3-[(3,5-dibromo-2-ethoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
98.2% inhibition at 50 nM
2-([3-[(3,5-dibromo-2-ethoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
Q38C91
-
2-([3-[(3,5-dibromo-2-methoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
95.0% inhibition at 50 nM
2-([3-[(3,5-dibromo-2-methoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
Q38C91
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
-
IC50 is 580 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1H-indole-3-carbonitrile
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1H-indole-3-carbonitrile
-
IC50 is 54 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-6-phenylpyrimidin-4(1H)-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-6-phenylpyrimidin-4(1H)-one
-
IC50 is 0.001 mM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 8.1 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
98.8% inhibition at 50 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-d]pyrimidin-4(1H)-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-d]pyrimidin-4(1H)-one
-
IC50 is 150 nM
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 3.9 nM
2-([3-[(3,5-dichlorobenzyl)amino]propyl]amino)-4a,8a-dihydroquinolin-4(1H)-one
Q38C91
-
2-([3-[(3,5-dichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
99.2% inhibition at 50 nM
2-([3-[(3,5-difluorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
45.8% inhibition at 50 nM
2-([3-[(3,5-dimethoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
35.3% inhibition at 50 nM
2-([3-[(3,5-dimethylbenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
91.1% inhibition at 50 nM
2-([3-[(3-bromobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
82.7% inhibition at 50 nM
2-([3-[(3-chlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
97.3% inhibition at 50 nM
2-([3-[(3-ethoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
19.1% inhibition at 50 nM
2-([3-[(4-chlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
52.0% inhibition at 50 nM
2-([3-[(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 14 nM
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 8.2 nM
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
-
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 17 nM
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
-
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
2-aminoquinolin-8-ol
Q38C91
-
2-chloro-4-[(4-methoxybenzyl)oxy]quinoline
-
-
2-[(3-[[3,5-bis(trifluoromethyl)benzyl]amino]propyl)amino]quinolin-4(1H)-one
-
36.9% inhibition at 50 nM
2-[(3-[[3-(trifluoromethoxy)benzyl]amino]propyl)amino]quinolin-4(1H)-one
-
56.5% inhibition at 50 nM
2-[2-allyloxy-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
-
2-[2-amino-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one tri(trifluoroacetic acid)
-
-
2-[2-benzyloxy-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-1-hydroxymethylpropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-dimethylaminopropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-ethoxypropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-hydroxymethylpropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-hydroxypropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-isopropoxy-propylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-methoxymethylpropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-methoxypropylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-2-propylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-4-hydroxybutylamino]-1H-quinolin-4-one
-
-
2-[3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
-
2-[3-[(3,4-dichlorobenzyl)amino]propoxy]quinolin-4(1H)-one
-
-
2-[3-[(3,4-dichlorobenzyl)amino]propoxy]quinolin-4(1H)-one
-
IC50 is 38 nM
2-[3-[bis-(3,4-dichlorobenzyl)-amino]-2-dimethylamino-propylamino]-1H-quinolin-4-one
-
-
2-[[3-(benzylamino)propyl]amino]quinolin-4(1H)-one
-
9.0% inhibition at 50 nM
3-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-1,4-dihydronaphthalen-1-ol
-
-
3-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-1,4-dihydronaphthalen-1-ol
-
IC50 is 0.0018 mM
3-[([3-[(4-oxo-1,4-dihydroquinolin-2-yl)amino]propyl]amino)methyl]benzonitrile
-
20.2% inhibition at 50 nM
4-methoxybenzyloxy-quinoline
-
-
4-[(E)-[([[N-(thiophen-2-ylcarbonyl)glycyl]amino]methyl)imino]methyl]benzoic acid
-
structure molecular modeling, binding mode, detailed overview
4-[3-(3,4-dichlorobenzylamino)propylamino]-1H-quinolin-2-one
-
-
4-[4-[(1H-benzimidazol-2-ylmethyl)amino]-6-(2-chloro-4-methoxyphenoxy)pyrimidin-2-yl]piperazin-2-one
Q38C91
-
5-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-b]pyridin-7(4H)-one
-
-
5-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-b]pyridin-7(4H)-one
-
IC50 is 4 nM
6-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-b]pyridin-4(7H)-one
-
-
6-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-b]pyridin-4(7H)-one
-
IC50 is 6.2 nM
actinomycin D
-
inhibits the nucleolar located enzyme due to dependence on polymerase I
adenosine
-
maximal inhibition at MgCl2 concentration from 4.0 mM to 10 mM, effective inhibition at high concentration of diphosphate
alpha-Amanitin
-
inhibits the nucleolar located enzyme due to dependence on polymerase I
ATP
-
in free form
benzoic acid 1-[(3,4-dichlorobenzylamino)-methyl]-2-(4-oxo-1,4-dihydroquinolin-2-ylamino)-ethyl ester
-
-
cisplatin
-
inhibits the nucleolar located enzyme due to dependence on polymerase I
D-methionine
-
-
EDTA
-
10 mM, weak
ester analogues of L-methionyl adenylate
-
overview, modeling of interaction with the active site
Ethionine
-
methionyl-tRNA formation
glutathione
-
-
hydroxamate analogues of L-methionyl adenylate
-
overview, modeling of the interaction with the active site
iodoacetamide
-
10 mM, weak
isovanilloid analogues of L-methionyl adenylate
-
overview, containing ribose biooisosteres
L-6,6,6-trifluoronorleucine
-
L-methionine analogue, competitive
L-cis-alpha-crotylglycine
-
L-methionine analogue, competitive
L-methionine hydroxamate
-
substrate analogue, inhibition mechanism, no inhibition of mutant T10M
L-norleucine
-
L-methionine analogue, competitive
L-norvaline
-
L-methionine analogue, competitive
L-trans-alpha-crotylglycine
-
L-methionine analogue, competitive
methionine
-
selenomethionyl-tRNA formation
N-(1,4-dihydroquinolin-2-yl)-N'-(2,3,5-trichlorobenzyl)propane-1,3-diamine
-
-
N-(1,4-dihydroquinolin-2-yl)-N'-(2,3,5-trichlorobenzyl)propane-1,3-diamine
-
IC50 is 0.0001 mM
N-(1H-benzimidazol-2-yl)-N'-(3,5-dichlorobenzyl)propane-1,3-diamine
Q38C91
-
N-(3,5-dibromobenzyl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-(3,5-dibromobenzyl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 5.0 nM
N-(6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-(6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 11 nM
N-(6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 18 nM
N-1H-benzimidazol-2-yl-N'-(2,4-dibromo-6-ethoxybenzyl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(2,4-dibromo-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is 17 nM
N-1H-benzimidazol-2-yl-N'-(2,4-dichloro-6-ethoxybenzyl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(2,4-dichloro-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is below 3 nM
N-1H-benzimidazol-2-yl-N'-(2-bromo-4-chloro-6-ethoxybenzyl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(2-bromo-4-chloro-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is 3.8 nM
N-1H-benzimidazol-2-yl-N'-(2-bromo-6-ethoxy-4-methoxybenzyl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(2-bromo-6-ethoxy-4-methoxybenzyl)propane-1,3-diamine
-
IC50 is 17 nM
N-1H-benzimidazol-2-yl-N'-(3,5-dibromobenzyl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(3,5-dibromobenzyl)propane-1,3-diamine
-
IC50 is 29 nM
N-1H-benzimidazol-2-yl-N'-(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
IC50 is 14 nM
N-1H-benzimidazol-2-yl-N'-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
-
N-1H-benzimidazol-2-yl-N'-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
IC50 is 16 nM
N-[(4R)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-[(4R)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 6.3 nM
N-[(4S)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
-
N-[(4S)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 48 nM
NaF
-
10 mM, weak
NH4+
-
ATP-diphosphate exchange
O-acetylserine
-
-
p-chloromercuribenzoate
-
-
Periodate-oxidized ATP
-
-
-
Periodate-oxidized tRNA
-
-
-
REP3123
-
active against a collection of 108 clinical isolates of Clostridium difficile and against epidemic, moxifloxacin-resistant BI/NAP1/027 strains
REP3123
Q181D9
a selective and potent competitive, versus methionine not ATP, MetRS inhibitor, that strongly binds at the active site, docking study
RNase
-
inhibits the nucleolar located enzyme due to dependence on rRNA
-
selenomethionine
-
methionyl-tRNA formation
vanilloid analogues of L-methionyl adenylate
-
overview, containing ribose biooisosteres
[1-[(3,4-dichlorobenzylamino)-methyl]-2-(4-oxo-1,4-dihydroquinolin-2-ylamino)ethyl]-carbamic acid tert-butyl ester
-
-
[3-[4-(4-Methoxy-benzyloxy)-quinolin-2-ylsulfanyl]-propyl]-carbamic acid tert-butyl ester
-
-
Mg2+
-
in free form
additional information
-
structure-activity relationships of inhibitor derived from an oxazolone-dipeptide scaffold
-
additional information
-
antibacterial potency of the inhibitors, structure-activity relationships, inhibition mechanism, the quinolone moiety of the right hand side pharmacophore is crucial for enzyme inhibition, overview
-
additional information
-
inhibition mechanism, the quinolone moiety of the right hand side pharmacophore is crucial for enzyme inhibition, overview
-
additional information
-
antibacterial potency of the inhibitors, structure-activity relationships, inhibition mechanism, the quinolone moiety of the right hand side pharmacophore is crucial for enzyme inhibition, overview
-
additional information
-
inhibition mechanism, the quinolone moiety of the right hand side pharmacophore is crucial for enzyme inhibition, overview
-
additional information
-
in vitro minimum inhibitory concentrations of quinoline compounds with different strains of Staphylococcus aureus, structure-activity relationships
-
additional information
-
large scale MetRS inhibitor screening, diverse compounds, overview
-
additional information
-
inhibitor screening, hstructures, omology modeling, molecular docking studies, and computational development of pharmacophore models, overview; inhibitor screening, structures, homology modeling, molecular docking studies, and computational development of pharmacophore models, overview
-
additional information
-
a homology model of the Trypanosoma brucei MetRS based on other MetRS structures is used to model binding of lead diaryl diamine compounds in the design and development of selective parasite MetRS inhibitors for treatment of African trypanosomiasis, overview
-
additional information
Q181D9
MetRS drug design and homology modelling, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12 kDa protein 2
Q9V011
the recombinant 12 kDa protein 2 plays an important role in dimerization of the enzyme
-
5SrRNA
-
positive effector of MetRS, markedly enhances the MetRS activity in the MetRS complex
-
5SrRNA
-
5SrRNA may be present as 5SrRNA-L5 protein complex; positive effector of MetRS, markedly enhances the MetRS activity in the MetRS complex
-
Arc1p
P00958
accessory protein Arc1p, SwissProt ID P46672
-
Arc1p-N
P00958
residues 1-122 of Arc1p, recombinantly expressed, crystal structure analysis, three interacting domains, MetRS-N-Arc1p-N hetero-dimer resembles a classical GST homo-dimer, overview; residues 1-122 of Arc1p, recombinantly expressed, crystal structure analysis, three interacting domains, MetRS-NArc1p-N hetero-dimer resembles a classical GST homo-dimer, overview
-
cysteic acid
-
stimulates
cysteine
-
stimulates
polymerase I
-
required by the nucleolar located enzyme
-
rRNA
-
required by the nucleolar located enzyme
SO32-
-
stimulates
spermine
P56192
slight stimulation, additionally spermine increases the enzyme activity by stabilizing conformation of negatively charged DNA
elongation factor EF-1alpha
-
activates, assists in dissociation of Met-tRNAMet from the enzyme, the aminoacylated tRNA is transfered from to the enzyme to the elongation factor
-
additional information
P56192
bovine serum albumin has no effect on the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.68
(S)-2-aminohex-5-enoic acid
-
ATP-diphosphate exchange reaction, pH 7.6
2.42
(S)-2-aminohex-5-ynoic acid
-
ATP-diphosphate exchange reaction, pH 7.6
0.085
ATP
P56192
pH 8.2, 37C, recombinant enzyme
0.085
ATP
-
-
0.09
ATP
Lupinus sp.
-
-
0.18
ATP
-
-
0.3
ATP
-
ligase B
0.375
ATP
-
wild-type, first step of reaction, methionyl-adenylate formation
0.41
ATP
-
strain 547, ATP-diphosphate exchange
0.44
ATP
-
mutant G54S, first step of reaction, methionyl-adenylate formation
0.475
ATP
-
mutant H101N/G213C, first step of reaction, methionyl-adenylate formation
0.5
ATP
-
mutant G54S, ATP:diphosphate exchange reaction; wild-type, ATP:diphosphate exchange reaction
0.55
ATP
-
ATP-diphosphate exchange
0.595
ATP
-
mutant L213W, ATP:diphosphate exchange reaction
0.6
ATP
-
ligase A
0.65
ATP
-
mutant V108M, ATP:diphosphate exchange reaction
0.7
ATP
-
mutant H101D, first step of reaction, methionyl-adenylate formation
0.75
ATP
-
mutant G223C, ATP:diphosphate exchange reaction
0.76
ATP
-
mutant G54A/A64P, ATP:diphosphate exchange reaction
0.765
ATP
-
mutant I57N/G54S, ATP:diphosphate exchange reaction
0.78
ATP
-
mutant V216A, first step of reaction, methionyl-adenylate formation
0.81
ATP
-
mutant I57N/V242F, ATP:diphosphate exchange reaction
0.82
ATP
-
mutant I57N, ATP:diphosphate exchange reaction
0.85
ATP
-
mutant V216F/L203S, first step of reaction, methionyl-adenylate formation
0.98
ATP
-
mutant D229E, first step of reaction, methionyl-adenylate formation
1
ATP
-
mutant I57N, first step of reaction, methionyl-adenylate formation
1.14
ATP
-
mutant A247E, ATP:diphosphate exchange reaction
1.3
ATP
-
ATP-diphosphate exchange
1.35
ATP
-
mutant G54S/L203S, first step of reaction, methionyl-adenylate formation
1.61
ATP
-
mutant I57N/I238F, ATP:diphosphate exchange reaction
1.75
ATP
-
mutant I57N/H101N, first step of reaction, methionyl-adenylate formation
2.23
ATP
-
mutant I57N/A247E, ATP:diphosphate exchange reaction
7.9
ATP
-
wild-type, pH 7.5, 37C
58
ATP
-
mutant T10M, pH 7.5, 37C
1.2
CoA
-
methionylation reaction, cytoplasmic isozyme, pH 7.8, 25C
6.3
CoA
-
methionylation reaction, mitochondrial isozyme, pH 7.8, 25C
1.8
L-homocysteine
-
editing reaction, mitochondrial isozyme, pH 7.8, 25C
3.1
L-homocysteine
-
editing reaction, cytoplasmic isozyme, pH 7.8, 25C
0.027
L-Met
-
-
0.133
L-Met
-
ATP-diphosphate exchange, enzyme form B
0.166
L-Met
-
ATP-diphosphate exchange, enzyme form A
0.26
L-Met
-
-
0.006
L-methionine
-
mutant I57N, first step of reaction, methionyl-adenylate formation
0.017
L-methionine
-
mutant V216A, first step of reaction, methionyl-adenylate formation
0.018
L-methionine
P56192
pH 8.2, 37C, recombinant enzyme
0.02
L-methionine
-
-
0.02
L-methionine
-
mutant I57N/V242F, ATP:diphosphate exchange reaction
0.0243
L-methionine
-
ATP-diphosphate exchange reaction, pH 7.6
0.025
L-methionine
-
mutant I57N, ATP:diphosphate exchange reaction
0.025
L-methionine
-
mutant V216F/L203S, first step of reaction, methionyl-adenylate formation; wild-type, first step of reaction, methionyl-adenylate formation
0.053
L-methionine
-
-
0.055
L-methionine
-
mutant G54S/L203S, first step of reaction, methionyl-adenylate formation
0.075
L-methionine
-
mutant G54S, ATP:diphosphate exchange reaction
0.085
L-methionine
-
mutant I57N/I238F, ATP:diphosphate exchange reaction
0.092
L-methionine
-
mutant D229E, first step of reaction, methionyl-adenylate formation
0.1
L-methionine
-
mutant L213W, ATP:diphosphate exchange reaction; wild-type, ATP:diphosphate exchange reaction
0.14
L-methionine
-
mutant V108M, ATP:diphosphate exchange reaction
0.16
L-methionine
-
mutant G54S, first step of reaction, methionyl-adenylate formation
0.19
L-methionine
-
mutant I57N/H101N, first step of reaction, methionyl-adenylate formation
0.22
L-methionine
-
mutant A247E, ATP:diphosphate exchange reaction
0.25
L-methionine
-
-
0.25
L-methionine
-
mutant I57N/A247E, ATP:diphosphate exchange reaction
0.36
L-methionine
-
mutant I57N/G54S, ATP:diphosphate exchange reaction
0.68
L-methionine
-
mutant G223C, ATP:diphosphate exchange reaction
1.07
L-methionine
-
mutant G54A/A64P, ATP:diphosphate exchange reaction
1.55
L-methionine
-
mutant H101N/G213C, first step of reaction, methionyl-adenylate formation
7.9
L-methionine
-
wild-type, pH 7.5, 37C
14.8
L-methionine
-
mutant H101D, first step of reaction, methionyl-adenylate formation
58
L-methionine
-
mutant T10M, pH 7.5, 37C
4.12
L-norleucine
-
ATP-diphosphate exchange reaction, pH 7.6
4.56
L-trans-alpha-crotylglycine
-
ATP-diphosphate exchange reaction, pH 7.6
0.015
Met
Lupinus sp.
-
-
0.018
Met
-
ligase A and B
0.02
Met
-
strain 547, ATP-diphosphate exchange
0.022
Met
-
methionine-dependent ATP-diphosphate exchange
0.032
Met
-
methionine-dependent ATP-diphosphate exchange
0.078
Met
-
wild-type enzyme
0.383
norleucine
-
-
28.6
norleucine
-
-
0.038
selenomethionine
-
selenomethionine-dependent ATP-diphosphate exchange
0.31
selenomethionine
-
-
0.0007
tRNA fraction from Saccharomyces cerevisiae
Q9ZTS1
pH 7.5, 25C, wild-type enzyme
-
0.00075
tRNA fraction from Saccharomyces cerevisiae
Q9ZTS1
pH 7.5, 25C, truncated mutant
-
0.00015
tRNAMet
P56192
pH 8.2, 37C, mitochondrial tRNAMet from Bos taurus, recombinant enzyme
0.00016
tRNAMet
P56192
pH 8.2, 37C, human mitochondrial wild-type tRNAMet, recombinant enzyme
0.00025
tRNAMet
Lupinus sp.
-
-
0.00027
tRNAMet
-
mutant G54S, aminoacylation reaction
0.0004
tRNAMet
-
recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25C
0.00041
tRNAMet
-
mutant I57N/G54S, aminoacylation reaction
0.00045
tRNAMet
-
mutant I57N/A247E, aminoacylation reaction
0.00055
tRNAMet
-
wild-type, second step of reaction, tRNA aminoacylation
0.00057
tRNAMet
-
mutant G54A/A64P, aminoacylation reaction
0.00064
tRNAMet
-
mutant G54S/L203S, second step of reaction, tRNA aminoacylation
0.00065
tRNAMet
-
mutant D229E, second step of reaction, tRNA aminoacylation
0.00066
tRNAMet
Q9ZTS1
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25C, wild-type enzyme
0.0008
tRNAMet
-
mutant V216A, second step of reaction, tRNA aminoacylation
0.00089
tRNAMet
-
mutant I57N/I238F, aminoacylation reaction
0.0009
tRNAMet
-
wild-type enzyme
0.00093
tRNAMet
-
mutant I57N, aminoacylation reaction
0.00096
tRNAMet
-
mutant V216F/L203S, second step of reaction, tRNA aminoacylation
0.001
tRNAMet
-
wild-type, aminoacylation reaction
0.001
tRNAMet
-
-
0.00102
tRNAMet
-
mutant G54S, second step of reaction, tRNA aminoacylation
0.00121
tRNAMet
-
mutant I57N/H101N, second step of reaction, tRNA aminoacylation
0.0013
tRNAMet
-
mutant A247E, aminoacylation reaction
0.0014
tRNAMet
-
-
0.0017
tRNAMet
-
mutant L213W, aminoacylation reaction
0.0021
tRNAMet
P56192
pH 8.2, 37C, initiator tRNA from Escherichia coli, recombinant enzyme
0.0022
tRNAMet
-
C-terminal extension, pH 7.5, 25C
0.0025
tRNAMet
-
mutant G223C, aminoacylation reaction
0.0026
tRNAMet
-
mutant I57N, second step of reaction, tRNA aminoacylation
0.0032
tRNAMet
-
substrate from Escherichia coli, 37C
0.0032
tRNAMet
-
mutant V108M, aminoacylation reaction
0.0033
tRNAMet
-
mutant K863A, pH 7.5, 25C
0.0035
tRNAMet
-
wild-type enzyme, pH 7.5, 25C
0.0039
tRNAMet
-
wild-type enzyme in the multi-enzyme complex and mutant K866A, pH 7.5, 25C
0.0039
tRNAMet
-
pH 7.5, 25C, wild-type enzyme
0.0044
tRNAMet
-
aminoacylation reaction, wild-type
0.0057
tRNAMet
-
mutant R857A, pH 7.5, 25C
0.0058
tRNAMet
-
aminoacylation reaction, C-terminally truncated mutant
0.006
tRNAMet
-
pH 7.5, 25C, mutant D369K/K295D
0.0064
tRNAMet
-
aminoacylation reaction, mutant D666A
0.0065
tRNAMet
Q9ZTS1
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25C, truncated mutant
0.0087
tRNAMet
-
aminoacylation reaction, mutant M665
0.009
tRNAMet
-
recombinant cytoplasmic isozyme, pH 7.8, 25C
0.01
tRNAMet
-
mutant I57N/V242F, aminoacylation reaction
0.0102
tRNAMet
-
pH 7.5, 25C, mutant KA295V
0.015
tRNAMet
-
recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25C
0.0163
tRNAMet
-
mutant K880A, pH 7.5, 25C
0.0172
tRNAMet
-
mutant K860A, pH 7.5, 25C
0.0177
tRNAMet
-
pH 7.5, 25C, mutant K295V
0.018
tRNAMet
-
pH 7.5, 25C, mutant D369A
0.02
tRNAMet
-
ATP-diphosphate exchange reaction, wild-type
0.022
tRNAMet
-
ATP-diphosphate exchange reaction, C-terminally truncated mutant
0.026
tRNAMet
-
pH 7.5, 25C, mutant D369N
0.029
tRNAMet
-
ATP-diphosphate exchange reaction, mutant D666A
0.032
tRNAMet
-
catalytic domain, pH 7.5, 25C
0.034
tRNAMet
-
ATP-diphosphate exchange reaction, mutant M665
1
tRNAMet
-
recombinant C-terminally truncated enzyme, 37C
0.48 - 1.63
Met
-
Km-values of various mutant strains
additional information
additional information
-
Km-values of mutant enzymes in ATP-diphosphate exchange reaction
-
additional information
additional information
-
Km-values of mutant enzymes in aminoacylation
-
additional information
additional information
-
dissociation constants for wild-type and mutant enzymes
-
additional information
additional information
-
kinetics with Escherichia coli native tRNAMet and initiator tRNAMet, and Saccharomyces cerevisiae native tRNAMet and initiator tRNAMet, overview
-
additional information
additional information
-
steady-state kinetic parameters for tRNAMet aminoacylation and for MetRS-catalyzed diphosphate exchange of wild-type enzyme and mutants, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.35
(S)-2-aminohex-5-enoic acid
-
ATP-diphosphate exchange reaction, pH 7.6
2.6
(S)-2-aminohex-5-ynoic acid
-
ATP-diphosphate exchange reaction, pH 7.6
0.033
ATP
P56192
pH 8.2, 37C, recombinant enzyme
3.4
ATP
-
mutant T10M, pH 7.5, 37C
5.6
ATP
-
wild-type, pH 7.5, 37C
0.7
CoA
-
methionylation reaction, cytoplasmic isozyme, pH 7.8, 25C
1.6
CoA
-
methionylation reaction, mitochondrial isozyme, pH 7.8, 25C
0.5
L-homocysteine
-
editing reaction, mitochondrial isozyme, pH 7.8, 25C
0.69
L-homocysteine
-
editing reaction, cytoplasmic isozyme, pH 7.8, 25C
6.08
L-homocysteine
-
editing reaction, cytoplasmic isozyme, pH 7.8, 25C
2.94
L-Met
-
ATP-diphosphate exchange, enzyme form A
3.13
L-Met
-
ATP-diphosphate exchange, enzyme form B
0.41
L-methionine
P56192
pH 8.2, 37C, recombinant enzyme
1
L-methionine
-
mutant G54A/A64P, ATP:diphosphate exchange reaction
3.4
L-methionine
-
mutant T10M, pH 7.5, 37C
4
L-methionine
-
mutant G54S, first step of reaction, methionyl-adenylate formation
5
L-methionine
-
mutant G54S, ATP:diphosphate exchange reaction
5.6
L-methionine
-
wild-type, pH 7.5, 37C
6
L-methionine
-
mutant I57N/G54S, ATP:diphosphate exchange reaction
6
L-methionine
-
mutant I57N/H101N, first step of reaction, methionyl-adenylate formation
8
L-methionine
-
mutant H101N/G213C, first step of reaction, methionyl-adenylate formation
10
L-methionine
-
mutant G223C, ATP:diphosphate exchange reaction; mutant L213W, ATP:diphosphate exchange reaction
11
L-methionine
-
mutant A247E, ATP:diphosphate exchange reaction; mutant I57N/A247E, ATP:diphosphate exchange reaction
13
L-methionine
-
mutant I57N/I238F, ATP:diphosphate exchange reaction
13.3
L-methionine
-
ATP-diphosphate exchange reaction, pH 7.6
14
L-methionine
-
mutant I57N, ATP:diphosphate exchange reaction; mutant I57N/V242F, ATP:diphosphate exchange reaction
15
L-methionine
-
mutant V108M, ATP:diphosphate exchange reaction
15
L-methionine
-
mutant G54S/L203S, first step of reaction, methionyl-adenylate formation; mutant H101D, first step of reaction, methionyl-adenylate formation; mutant I57N, first step of reaction, methionyl-adenylate formation
23
L-methionine
-
wild-type, first step of reaction, methionyl-adenylate formation
25
L-methionine
-
wild-type, ATP:diphosphate exchange reaction
25
L-methionine
-
mutant V216A, first step of reaction, methionyl-adenylate formation; mutant V216F/L203S, first step of reaction, methionyl-adenylate formation
33
L-methionine
-
mutant D229E, first step of reaction, methionyl-adenylate formation
2.15
L-norleucine
-
ATP-diphosphate exchange reaction, pH 7.6
1.82
L-trans-alpha-crotylglycine
-
ATP-diphosphate exchange reaction, pH 7.6
2.94
L-trans-alpha-crotylglycine
-
ATP-diphosphate exchange reaction, pH 7.6
0.26
tRNA fraction from Saccharomyces cerevisiae
Q9ZTS1
pH 7.5, 25C, truncated mutant
-
0.53
tRNA fraction from Saccharomyces cerevisiae
Q9ZTS1
pH 7.5, 25C, wild-type enzyme
-
6.08
tRNA fraction from Saccharomyces cerevisiae
Q9ZTS1
pH 7.5, 25C, wild-type enzyme
-
0.001
tRNAMet
-
mutant G54A/A64P, aminoacylation reaction
0.002
tRNAMet
-
mutant I57N/G54S, aminoacylation reaction
0.006
tRNAMet
-
mutant V216F/L203S, second step of reaction, tRNA aminoacylation
0.008
tRNAMet
-
mutant I57N/A247E, aminoacylation reaction
0.009
tRNAMet
-
mutant G54S, aminoacylation reaction
0.01
tRNAMet
-
mutant G54S, second step of reaction, tRNA aminoacylation
0.011
tRNAMet
-
mutant G54S/L203S, second step of reaction, tRNA aminoacylation
0.013
tRNAMet
-
mutant I57N/H101N, second step of reaction, tRNA aminoacylation
0.017
tRNAMet
-
mutant I57N, second step of reaction, tRNA aminoacylation
0.019
tRNAMet
P56192
pH 8.2, 37C, mitochondrial tRNAMet from Bos taurus, recombinant enzyme
0.021
tRNAMet
P56192
pH 8.2, 37C, human mitochondrial wild-type tRNAMet, recombinant enzyme
0.023
tRNAMet
-
mutant I57N, aminoacylation reaction
0.023
tRNAMet
-
mutant D229E, second step of reaction, tRNA aminoacylation
0.037
tRNAMet
-
mutant G223C, aminoacylation reaction
0.037
tRNAMet
-
pH 7.5, 25C, mutant D369A
0.042
tRNAMet
-
pH 7.5, 25C, mutant KA295V
0.05
tRNAMet
-
pH 7.5, 25C, mutant D369K/K295D
0.055
tRNAMet
-
mutant V216A, second step of reaction, tRNA aminoacylation
0.057
tRNAMet
-
mutant A247E, aminoacylation reaction
0.066
tRNAMet
-
mutant I57N/I238F, aminoacylation reaction
0.08
tRNAMet
-
wild-type, second step of reaction, tRNA aminoacylation
0.09
tRNAMet
-
C-terminal extension, pH 7.5, 25C
0.11
tRNAMet
-
pH 7.5, 25C, mutant D369N
0.124
tRNAMet
-
mutant I57N/V242F, aminoacylation reaction
0.15
tRNAMet
-
wild-type enzyme, pH 7.5, 25C
0.2
tRNAMet
-
recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25C
0.22
tRNAMet
-
mutant K863A, pH 7.5, 25C
0.23
tRNAMet
-
mutant K866A, pH 7.5, 25C
0.29
tRNAMet
Q9ZTS1
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25C, wild-type enzyme
0.3
tRNAMet
-
pH 7.5, 25C, mutant K295V
0.36
tRNAMet
Q9ZTS1
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25C, truncated mutant
0.46
tRNAMet
-
wild-type enzyme in the multi-enzyme complex, pH 7.5, 25C
0.47
tRNAMet
-
mutant R857A, pH 7.5, 25C
0.49
tRNAMet
-
wild-type, aminoacylation reaction
0.54
tRNAMet
-
mutant L213W, aminoacylation reaction
0.74
tRNAMet
-
mutant V108M, aminoacylation reaction
0.85
tRNAMet
-
mutant K860A, pH 7.5, 25C
1
tRNAMet
-
recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25C
1
tRNAMet
-
pH 7.5, 25C, wild-type enzyme
1.03
tRNAMet
-
mutant K880A, pH 7.5, 25C
1.3
tRNAMet
-
recombinant cytoplasmic isozyme, pH 7.8, 25C
2 - 8
tRNAMet
-
ATP-diphosphate exchange reaction, mutant M665
2.4
tRNAMet
-
catalytic domain, pH 7.5, 25C
2.8
tRNAMet
-
aminoacylation reaction, wild-type
2.83
tRNAMet
-
substrate from Escherichia coli, 37C
3 - 6
tRNAMet
-
substrate from Escherichia coli, 37C
3.1
tRNAMet
-
aminoacylation reaction, mutant D666A
3.3
tRNAMet
-
wild-type enzyme
3.6
tRNAMet
-
aminoacylation reaction, C-terminally truncated mutant
4.4
tRNAMet
-
aminoacylation reaction, mutant M665
6.08
tRNAMet
-
mutant K880A, pH 7.5, 25C
6.85
tRNAMet
-
recombinant C-terminally truncated enzyme, 37C
11
tRNAMet
P56192
pH 8.2, 37C, initiator tRNA from Escherichia coli, recombinant enzyme
23
tRNAMet
-
ATP-diphosphate exchange reaction, mutant D666A
42
tRNAMet
-
ATP-diphosphate exchange reaction, wild-type
47
tRNAMet
-
ATP-diphosphate exchange reaction, C-terminally truncated mutant
3 - 6
Met-tRNAMet
-
-
additional information
additional information
-
in ATP-diphosphate exchange reaction; turnover numbers of mutant enzymes
-
additional information
additional information
-
in aminoacylation; turnover numbers of mutant enzymes
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
tRNAMet
-
pH 7.5, 25C, mutant D369A
622
4
tRNAMet
-
pH 7.5, 25C, mutant D369N; pH 7.5, 25C, mutant KA295V
622
8
tRNAMet
-
pH 7.5, 25C, mutant D369K/K295D
622
17
tRNAMet
-
pH 7.5, 25C, mutant K295V
622
250
tRNAMet
-
pH 7.5, 25C, wild-type enzyme
622
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000017
REP3123
-
-
0.00000002
REP3123
-
wild-type
0.00000008
REP3123
-
MetRS1
0.0000002
REP3123
-
mutant I57N
0.00001
REP3123
-
mutant V216F/L203S
0.000013
REP3123
-
mutant G54S
0.000018
REP3123
-
mutant D229E
0.000028
REP3123
-
mitochondrial MetRS
0.00007
REP3123
-
mutant V216A
0.000155
REP3123
-
mutant I57N/H101N
0.000178
REP3123
-
-
0.000375
REP3123
-
mutant H101D
0.0005
REP3123
-
mutant G54S/L203S
0.001
REP3123
-
mutant H101N/G213C
0.0019
REP3123
-
-
0.02
REP3123
-
cytoplasmic MetRS
0.02
REP3123
-
MetRS2
0.00000001
REP8839
-
wild-type
0.00000004
REP8839
-
mutant L213W
0.000000055
REP8839
-
-
0.00000006
REP8839
-
mutant A247E
0.00000008
REP8839
-
mutant I57N
0.00000011
REP8839
-
mutant V108M
0.00000051
REP8839
-
mutant G223C
0.00001
REP8839
-
hmMetRS
0.000015
REP8839
-
mutant I57N/V242F
0.000023
REP8839
-
-
0.00006
REP8839
-
mutant I57N/A247E
0.000085
REP8839
-
mutant G54S
0.000225
REP8839
-
-
0.00035
REP8839
-
mutant I57N/I238F
0.0009
REP8839
-
mutant I57N/G54S
0.0019
REP8839
-
mutant G54A/A64P
0.02
REP8839
-
hcMetRS, larger than 0.020
0.0196
L-methionine hydroxamate
-
pH 8.0
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 40 nM
0.0035
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0035 mM
0.00017
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 170 nM
0.099
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.099 mM
0.00034
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 340 nM
0.0066
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0066 mM
0.000018
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 18 nM
0.0035
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0035 mM
0.00018
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 180 nM
0.0013
1-[1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0013 mM
0.000087
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 87 nM
0.001
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.001 mM
0.00076
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 760 nM
0.0031
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-butyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0031 mM
0.00167
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 1670 nM
0.1
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-ethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
0.00017
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 170 nM
0.099
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.099 mM
0.00085
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 850 nM
0.0059
1-[1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-propyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0059 mM
0.00007
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 70 nM
0.1
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
0.00068
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 680 nM
0.1
1-[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
0.00051
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 510 nM
0.1
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-azetidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is above 0.1 mM
0.0011
1-[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 1100 nM
0.00033
1-[3-[(3,5-dibromobenzyl)amino]propyl]-3-phenylurea
-
IC50 is 330 nM
0.00043
1-[[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 430 nM
0.027
1-[[2-(2,4-dichloro-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.027 mM
0.00081
1-[[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 810 nM
0.0061
1-[[2-(4-bromo-phenyl)-5-oxo-oxazol-4-ylidene]-phenyl-methyl]-pyrrolidine-2-carboxylic acid [1-carbamoyl-2-(4-hydroxy-phenyl)-ethyl]-amide
-
IC50 is 0.0061 mM
0.001
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-4H-chromen-4-one
-
IC50 is 0.001 mM
0.0000003
2-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
IC50 is below 0.3 nM
0.0000097
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 9.7 nM
0.0000049
2-([3-[(2,4-dibromo-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 4.9 nM
0.000003
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is below 3 nM
0.000003
2-([3-[(2,4-dichloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
0.000003
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is below 3 nM
0.000003
2-([3-[(2-bromo-4-chloro-6-ethoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
0.000007
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 7.0 nM
0.0000033
2-([3-[(2-bromo-6-ethoxy-4-methoxybenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 3.3 nM
0.00068
2-([3-[(3,4-dichlorobenzyl)amino]propyl]thio)quinolin-4(1H)-one
-
IC50 is 680 nM
0.000013
2-([3-[(3,5-dibromo-2-ethoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
Q38C91
pH and temperature not specified in the publication
0.000065
2-([3-[(3,5-dibromo-2-methoxybenzyl)amino]propyl]amino)quinolin-4(1H)-one
Q38C91
pH and temperature not specified in the publication
0.00058
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
-
IC50 is 580 nM
0.000054
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-1H-indole-3-carbonitrile
-
IC50 is 54 nM
0.001
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)-6-phenylpyrimidin-4(1H)-one
-
IC50 is 0.001 mM
0.0000081
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 8.1 nM
0.000003
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)quinolin-4(1H)-one
-
IC50 is below 3 nM
0.00015
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-d]pyrimidin-4(1H)-one
-
IC50 is 150 nM
0.0000039
2-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 3.9 nM
0.000008
2-([3-[(3,5-dichlorobenzyl)amino]propyl]amino)-4a,8a-dihydroquinolin-4(1H)-one
Q38C91
pH and temperature not specified in the publication
0.000014
2-([3-[(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is 14 nM
0.0000082
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 8.2 nM
0.000003
2-([3-[(7-bromo-5-chloro-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
0.000017
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)quinazolin-4(1H)-one
-
IC50 is 17 nM
0.000003
2-([3-[(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)amino]propyl]amino)thieno[3,2-d]pyrimidin-4(1H)-one
-
IC50 is below 3 nM
0.0000294
2-[2-allyloxy-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
-
0.000102
2-[2-amino-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one tri(trifluoroacetic acid)
-
-
0.0000247
2-[2-benzyloxy-3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
-
0.0000186
2-[3-(3,4-dichlorobenzylamino)-1-hydroxymethylpropylamino]-1H-quinolin-4-one
-
-
0.0000396
2-[3-(3,4-dichlorobenzylamino)-2-dimethylaminopropylamino]-1H-quinolin-4-one
-
-
0.0000303
2-[3-(3,4-dichlorobenzylamino)-2-ethoxypropylamino]-1H-quinolin-4-one
-
-
0.0000119
2-[3-(3,4-dichlorobenzylamino)-2-hydroxymethylpropylamino]-1H-quinolin-4-one
-
-
0.0000023
2-[3-(3,4-dichlorobenzylamino)-2-hydroxypropylamino]-1H-quinolin-4-one
-
-
0.000091
2-[3-(3,4-dichlorobenzylamino)-2-isopropoxy-propylamino]-1H-quinolin-4-one
-
-
0.000015
2-[3-(3,4-dichlorobenzylamino)-2-methoxymethylpropylamino]-1H-quinolin-4-one
-
-
0.0000025
2-[3-(3,4-dichlorobenzylamino)-2-methoxypropylamino]-1H-quinolin-4-one
-
-
0.0000034
2-[3-(3,4-dichlorobenzylamino)-2-propylamino]-1H-quinolin-4-one
-
-
0.0000029
2-[3-(3,4-dichlorobenzylamino)-4-hydroxybutylamino]-1H-quinolin-4-one
-
-
0.0000011
2-[3-(3,4-dichlorobenzylamino)-propylamino]-1H-quinolin-4-one
-
isozyme MRSA
0.000038
2-[3-[(3,4-dichlorobenzyl)amino]propoxy]quinolin-4(1H)-one
-
IC50 is 38 nM
0.000131
2-[3-[bis-(3,4-dichlorobenzyl)-amino]-2-dimethylamino-propylamino]-1H-quinolin-4-one
-
-
0.0018
3-([3-[(2,3,5-trichlorobenzyl)amino]propyl]amino)-1,4-dihydronaphthalen-1-ol
-
IC50 is 0.0018 mM
0.000237
4-[(E)-[([[N-(thiophen-2-ylcarbonyl)glycyl]amino]methyl)imino]methyl]benzoic acid
-
-
0.00495
4-[3-(3,4-dichlorobenzylamino)propylamino]-1H-quinolin-2-one
-
-
0.000043
4-[4-[(1H-benzimidazol-2-ylmethyl)amino]-6-(2-chloro-4-methoxyphenoxy)pyrimidin-2-yl]piperazin-2-one
Q38C91
pH and temperature not specified in the publication
0.000004
5-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[3,2-b]pyridin-7(4H)-one
-
IC50 is 4 nM
0.0000062
6-([3-[(3,5-dibromobenzyl)amino]propyl]amino)thieno[2,3-b]pyridin-4(7H)-one
-
IC50 is 6.2 nM
0.0000694
benzoic acid 1-[(3,4-dichlorobenzylamino)-methyl]-2-(4-oxo-1,4-dihydroquinolin-2-ylamino)-ethyl ester
-
-
0.0001
N-(1,4-dihydroquinolin-2-yl)-N'-(2,3,5-trichlorobenzyl)propane-1,3-diamine
-
IC50 is 0.0001 mM
0.000046
N-(1H-benzimidazol-2-yl)-N'-(3,5-dichlorobenzyl)propane-1,3-diamine
Q38C91
pH and temperature not specified in the publication
0.000005
N-(3,5-dibromobenzyl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 5.0 nM
0.000011
N-(6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 11 nM
0.000018
N-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 18 nM
0.000017
N-1H-benzimidazol-2-yl-N'-(2,4-dibromo-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is 17 nM
0.000003
N-1H-benzimidazol-2-yl-N'-(2,4-dichloro-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is below 3 nM
0.0000038
N-1H-benzimidazol-2-yl-N'-(2-bromo-4-chloro-6-ethoxybenzyl)propane-1,3-diamine
-
IC50 is 3.8 nM
0.000017
N-1H-benzimidazol-2-yl-N'-(2-bromo-6-ethoxy-4-methoxybenzyl)propane-1,3-diamine
-
IC50 is 17 nM
0.000029
N-1H-benzimidazol-2-yl-N'-(3,5-dibromobenzyl)propane-1,3-diamine
-
IC50 is 29 nM
0.000014
N-1H-benzimidazol-2-yl-N'-(5,7-dibromo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
IC50 is 14 nM
0.000016
N-1H-benzimidazol-2-yl-N'-(7-ethyl-5-iodo-1,2,3,4-tetrahydroquinolin-4-yl)propane-1,3-diamine
-
IC50 is 16 nM
0.0000063
N-[(4R)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 6.3 nM
0.000048
N-[(4S)-6,8-dibromo-1,2,3,4-tetrahydroquinolin-4-yl]-N'-1H-imidazo[4,5-b]pyridin-2-ylpropane-1,3-diamine
-
IC50 is 48 nM
0.000102
[1-[(3,4-dichlorobenzylamino)-methyl]-2-(4-oxo-1,4-dihydroquinolin-2-ylamino)ethyl]-carbamic acid tert-butyl ester
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.044
-
-
0.0462
Lupinus sp.
-
-
0.08
-
enzyme form B
0.087
-
-
0.09
-
enzyme form A
0.11
-
MettRNA
0.405
-
-
0.675
-
-
66.7
-
ATP-diphosphate exchange
additional information
-
incorporation level of L-methionine into proteins
additional information
Q9V011
-
additional information
-
activity with Escherichia coli native tRNAMet and initiator tRNAMet, and Saccharomyces cerevisiae native tRNAMet and initiator tRNAMet, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
sodium cacodylate or Tris buffer
7.2 - 7.9
-
ATP-diphosphate exchange
7.5
-
assay at
7.5
Q9ZTS1
assay at
7.5
O74634
assay at
7.5
-
assay at
7.6
Q9V011
assay at
7.8 - 8.2
P56192
-
7.8
-
tRNA aminoacylation assay
7.9
-
assay at
8 - 8.5
-
-
8
Lupinus sp.
-
-
8.1 - 8.4
-
aminoacylation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
tRNA aminoacylation assay at room temperature for 30 min for IC50 determinations
22
-
assay at room temperature
25
-
assay at
25
Q9ZTS1
assay at
25
-
assay at
30
O74634
assay at
30
-
tRNA aminoacylation assay at 30C for 1 to 7.5 min for initial rate determination
37
P56192
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42 - 60
Q9V011
the enzyme is nearly inactive at 25C, highest activity at 60C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
O23761, Q91UL7
a single gene of chloroplast origin codes for mitochondrial and chloroplastic isozyme, possessing a targeting signal sequence with dual function
Manually annotated by BRENDA team
-
the isozyme from chloroplasts is identical with the one from mitochondria
Manually annotated by BRENDA team
-
cytoplasmic enzyme form
Manually annotated by BRENDA team
-
cytoplasmic isozyme has a zinc-finger motif and an insertion domain that divides the nucleotide-binding fold into 2 halves
Manually annotated by BRENDA team
O74634
mitochondrial isozyme
Manually annotated by BRENDA team
O23761, Q91UL7
a single gene of chloroplast origin codes for mitochondrial and chloroplastic isozyme, possessing a targeting signal sequence with dual function
Manually annotated by BRENDA team
-
mitochondrial isozyme contains no zinc-finger motif and no insertion domain in the nucleotide-binding fold
Manually annotated by BRENDA team
-
the isozyme from mitochondria is identical with the one from chloroplasts
Manually annotated by BRENDA team
-
translocation from the cytoplasm is triggered by insulin, epidermal growth factor, translocation by a proliferation signal, the enzyme is part of the multi-aminoacyl-tRNA synthetase complex in the nucleolus
Manually annotated by BRENDA team
additional information
-
no enzyme in quiescent cells
-
Manually annotated by BRENDA team
additional information
O23761, Q91UL7
the in vitro synthesized enzyme is taken up by specific transport into chloroplasts of Pisum sativum, and in mitochondria of Solanum tuberosum, the imported protein becomes processed in both cases
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
Q9V011
recombinant 12 kDa protein 2, gel filtration
650114
58000
A0R3E2
determined by SDS-PAGE
701527
62000
Q9ZTS1
truncated enzyme, gel filtration
650978
62000
-
recombinant truncated mutant, mass spectrometry
653028
63000
-
ligase B, sucrose density gradient centrifugation
59
65000
-
enzyme form A, gel filtration
57
67000
P56192
gel filtration
661156
70000
-
gel filtration
65
80000
-
gel filtration
70
85000
-
enzyme form B, gel filtration
57
90000
-
enzyme form A, sucrose density gradient centrifugation
59
110000
Q9ZTS1
wild-type enzyme, gel filtration
650978
149000
-
recombinant wild-type enzyme, mass spectrometry
653028
165000
-
gel filtration
55
170000
Lupinus sp.
-
gel filtration
63
175000
-
PAGE under nondissociating conditions
67
340000
-
gel filtration
64
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 76127, calculation from nucleotide sequence
?
P56192
x * 100000, SDS-PAGE
?
O23761, Q91UL7
x * 62000, processed enzyme, SDS-PAGE
?
Q9V011
x * 84000, recombinant protein 1 expressed in Escherichia coli, SDS-PAGE
dimer
-
2 * 85000, SDS-PAGE after boiling the enzyme in 2% SDS and 1% mercaptoethanol, reduction and carboxymethylation in 6 M guanidine hydrochloride
dimer
-
2 * 76000
dimer
-
2 * 31000, enzyme form A, SDS-PAGE
dimer
-
2 * 74000, SDS-PAGE
dimer
-
2 * 75000, SDS-PAGE
dimer
Lupinus sp.
-
2 * 85000, SDS-PAGE
dimer
Q9V011
2 * 12000, recombinant protein 2 expressed in Escherichia coli, SDS-PAGE
dimer
-
recombinant wild-type, mass spectrometry
dimer
Escherichia coli EM
-
2 * 85000, SDS-PAGE after boiling the enzyme in 2% SDS and 1% mercaptoethanol, reduction and carboxymethylation in 6 M guanidine hydrochloride
-
monomer
A0R3E2
-
monomer
-
1 * 70000, ligase B, SDS-PAGE, 1 * 105000, ligase A, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 78000, SDS-PAGE, fully active monomeric enzyme derived from high-molecular-weight complexes by controlled proteolysis
monomer
P56192
1 * 67000, SDS-PAGE
monomer
-
1 * 62000, recombinant truncated mutant enzyme, mass spectrometry
monomer
Q9ZTS1
1 * 66500, truncated enzyme, SDS-PAGE, 1 * 89700, wild-type enzyme, SDS-PAGE
monomer
-
crystal structure determination
monomer
-
mutant D666A ia monomeric, M665 mutant is monomeic in absence of NgCl2, and dimeric in presence of 10 mM MgCl2, native PAGE
tetramer
-
4 * 85000, SDS-PAGE
tetramer
-
2 * 31000 + 2 * 10000, enzyme form B, SDS-PAGE
monomer
-
MetRs is a monomeric multidomain enzyme, comparisons with other MetRS structures. The MetRS core unit consists of four domains: the catalytic domain, the CP domain, the KMSKS domain, and an anticodon-binding domain.the enzyme crystal structure contains a KMSKS(301-305) loop in proximity to the catalytic site in an open and inactive conformation, overview
additional information
-
three-dimensional solution structure
additional information
Q9ZTS1
at high protein concentration the enzyme can form a dimer in vitro
additional information
Q9V011
dimerization of the enzyme is required for affinity to tRNAMet
additional information
P56192
domain structure, structure modeling based on crystal structures of Escherichia coli with PDB code 1QQR, overview, the enzyme contains the consensus motifs of class I aminoacyl-tRNA, but lacks the Zn2+ binding motif and the C-terminal dimerization region
additional information
-
structure analysis, catalytic Rossmann fold domain
additional information
Q9V011
three-dimensional structure, structure of the dimerization domain
additional information
P00958
MetRS shows domain swapping
additional information
-
three-dimensional structure of MetRS by homology modeling method, overview
additional information
-
homology modeling and ligand docking studies of trypanosomatid MetRS enzymes, structure comparisons, overview
additional information
-
MetRS is a multidomain protein, structural organization: the very C-terminal appended domain is related to the oligonucleotide binding-fold-based tRNA-binding domain recovered at the C-terminus of MetRS from plant, but, in the nematode enzyme, this domain is separated from the core enzyme by an insertion domain
additional information
Q181D9
secondary structure and three-dimensional structure molecular modeling, model validation, overview
additional information
-
structure of LmMetRS in complex with two products, methionyladenylate and diphosphate, along with a Mg2+ ion that bridges them, the residues of the class I aaRS signature sequence motifs, KISKS and HIGH, make numerous contacts with the diphosphate, structure comparisons, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme-mitochondrial tRNAMet complex with or without methionyl sulfamoyl adenosine, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
at 2.5 A resolution; crystals of active fragment of MW 64000 obtained by controlled proteolysis
-
crystal structure analysis, catalytic core, tertiary structure of the C-terminal tRNA-binding appendices determined by binding analysis of catalytically inactive tRNA homologous binding proteins: tRNA-binding protein 111 and endothelial monocyte-activating polypeptide II, i.e. EMAPII, comparison of structure with other aminoacyl tRNA synthetases from other organism
-
crystal structure determination by X-ray diffraction at 2.0 A resolution, 3D-structure of the C-terminally truncated enzyme, species-specific knuckle structures are determined
-
crystal structure of the tryptic fragment of the enzyme complexed with ATP, at 2.5 A resolution
-
crystals of active fragment of MW 64000 obtained by controlled proteolysis
-
crystals of purified free enzyme and enzyme complexed with L-methionine are diffused by several methionine analogues, i.e. L-difluoromethionine, L-trifluoromethionine, D,L-phosphomethionine and D,L-iodo-methionine, X-ray diffraction structure determination at 1.9 A resolution and analysis
-
purified enzyme complexed with L-methionine, protein solution: 8 mg/ml protein, 10 mM KH2PO4, pH 7.3, 10 mM 2-mercaptoethanol, initiating by microseeding with crystals from the free enzyme at 20C, in 1.1 ammonium citrate, 0.5% v/v methyl-2,4-pentanediol, 0.6 mM L-methionine, 2 mM 2-mercaptoethanol, 30 mM phosphate buffer, pH 7.0, 1 day, X-ray diffraction structure determination at 1.8 A resolution, structure analysis and modeling
-
the crystal structure of the mutated MetRS is determined in the apo form as well as complexed with methionine or azidonorleucine to 1.4 to 1.7 A resolution
-
truncated form
-
purified recombinant His-tagged catalytic core of methionyl-tRNA synthetase, containing a 3C protease cleavage site, in complex with the substrates MgATP2- and methionine, and in complex with two products, methionyladenylate and pyrophosphate, along with a Mg2+ ion that bridges them, hanging drop vapor diffusion, room temperature, 0.002 ml of 22 mg/ml protein in 25 mM HEPES, pH 7.0, 0.5 M NaCl, 0.025% sodium azide, 5% glycerol, 1 mM TCEP, 0.01 mM ZnCl2, 10 mM MgATP2- and 10 mM L-methionine, is mixed with 0.002 ml of reservoir solution containing 0.2 M potassium formate or potassium nitrate, pH 7.0-7.5, and 24-28% PEG 3350, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
monomeric MetRS in complex with the ligands methionine and adenosine or with methionine, X-ray diffraction structure determination and analysis at 2.3 A and 2.8 A resolution, respectively
-
the structure of methionyl-tRNA synthetase is determined to a resolution of 2.1 A
A0R3E2
purified recombinant M606 enzyme, hanging drop vapor diffusion method, from 0.1 M MES, pH 6.5, 3,5% PEG 6000, and 2% dioxane, 22C, 2 weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution
Q9V011
recombinant 12 kDa protein 2, 20% PEG 8000, cryoprotection in 10% ethylene glycol, 50 mM KH2PO4, X-ray diffraction structure determination at 2.0 A, and analysis
Q9V011
purified recombinant MetRS-N-Arc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 8-14% PEG 20000, 1-3% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution; purified recombinant MetRS-NArc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 814% PEG 20000, 13% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
P00958
crystal structure analysis, catalytic core, tertiary structure of the C-terminal tRNA-binding appendices determined by binding analysis of catalytically inactive tRNA homologous binding proteins: tRNA-binding protein 111 and endothelial monocyte-activating polypeptide II, i.e. EMAPII, comparison of structure with other aminoacyl tRNA synthetases from other organism
-
X-ray diffraction crystal structure determination at 2.0 A resolution and analysis
-
in complex with L-methionine and inhibitors, sitting drop vapor diffusion method, using 2.0-2.3 M (NH4)2SO4, 0.2 M NaCl, and 0.1 M sodium cacodylate (pH 6.0-6.6)
Q38C91
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51
-
wild-type enzyme, half-life 16 min
650114
additional information
-
thermostable enzyme
653028
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
several cycles of freezing and thawing, cause no loss of activity of wild-type enzyme in crude extract
-
bovine serum albumin has no effect on the enzyme
P56192
stability is increased by presence of a reducing agent. In the presence of 5 mM DTT purified enzyme is stable for at least 8 months at -15C
-
Mg2+, required for stability, enzyme loses 80% of its activity when stored at -20C for 3 days in buffer lacking Mg2+
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, about 35% loss of activity after 6 months, wild-type enzyme in crude extract
-
-20C, potassium phosphate buffer, pH 7.5, 50% glycerol, 1 mM dithioerythritol, stable for at least 6 months
-
-15C, 5 mM DTT, purified enzyme stable for at least 8 months
-
-20C, 50% v/v glycerol, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli
O74634
affinity chromatograph
-
affinity column chromatography
-
recombinant His-tagged mutant enzymes from strain DH10B by nickel affinity chromatography
-
recombinant His-tagged mutants from Escherichia coli strain XL-1 Blue by nickel affinity chromatography; recombinnat His-tagged mutants from Escherichia coli strain XL-1 Blue by nickel affinity chromatography
-
recombinant N-terminally His6-tagged MetRS monomer from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
the SLL-mutant is purified on columns containing Talon affinity resin and Q-Hiload resin, respectively
-
-
P56192
recombinant His-tagged mature enzyme form from Escherichia coli by ion exchange chromatography
P56192
recombinant wild-type enzyme, mutants and fragments from Escherichia coli
-
using Ni-nitrilotriacetic acid resin
-
recombinant His-tagged catalytic core of MetRS from Escherichia coli using the expression vector AVA0421 by nickel affinity chromatography and gel filtration
-
-
Lupinus sp.
-
Ni-NTA agarose is used, in addition gel filtration on a HiLoad 16/60 Superdex-200 column is applied
A0R3E2
two enzyme forms: A and B
-
glutathione-Sepharose 4B column chromatography
-
recombinant enzyme from Escherichia coli
Q9ZTS1
fully active monomeric enzyme derived from high-molecular-weight complexes by controlled proteolysis, trypsin-treatment
-
using Ni-affinity and SourceQ anion exchange chromatography
-
enzymes from chloroplasts and mitochondria, which are indistinguishable in the purificaion process, partial
-
recombinant M606 enzyme from Escherichia coli by ion exchange chromatography and gel filtration
Q9V011
aminoacyl-tRNA synthetase complex
-
recombinant GST-fusion protein of the mitochondrial isozyme
-
recombinant His-tagged MetRS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
P00958
by ammonium sulfate precipitation and anion-exchange chromatography on a Source 15Q column
-
two forms: ligase A and B
-
Ni-NTA affinity column chromatography and Superdex 75 gel filtration
Q38C91
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MetRS, phylogenetic analysis, the viral aminoacyl tRNA synthetases have not been acquired recently by horizontal gene transfer from a cellular host but rather militate in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes
-
DNA determination and analysis, overexpression in Escherichia coli SG13009, in vitro translation, expression of the enzyme as GFP-fusion protein in Nicotiana tabacum suspension cells
O23761, Q91UL7
genes metS1 and metS2, library construction, subcloning in Escherichia coli strains DH5alpha and INV110
-
DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli BL21(DE3), functional complementation of an enzyme-deficient Escherichia coli strain
O74634
expressed in Escherichia coli BL21(DE3) cells
-
expressed in HEK-293 cells
-
expression in an auxotroph Escherichia coli strain
-
expression of an N-terminally His6-tagged MetRS monomer in Escherichia coli strain BL21(DE3)
-
expression of His-tagged mutants in Escherichia coli strain XL-1 Blue
-
expression of mutant enzymes
-
gene metE, genetic library construction and expression, expression of His-tagged mutant enzymes in strains DH10B and in DH10B Met-
-
the unmutated monomeric versions of MetRS, truncated at residue 548, M547, is produced from the plasmid pBSM547, the pMTY21-sll plasmid codes for an N-terminally 6xHis-tagged M547 MetRS, leading to expression of the MetRS-SLL mutant
-
subcloning in Escherichia coli strain XL1-blue, expression in Haloferax volcanii
-
DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3) of the wild-type enzyme as His-tagged enzyme
-
expressed in HEK-293 cells
P56192
expression of the wild-type, and exchange mutant enzymes in Escherichia coli BL21(DE3), cloning and expression of the catalytic domain, amino acid residues A215-K823, and the C-terminal extension in Escherichia coli BL21(DE3)
-
mature enzyme form, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
P56192
plasmid pcDNA3.1MRS, containing a gene encoding hcMetRS, and plasmid pcDNA3.1MRSce2, containing a gene encoding full-length hmMetRS, are used, genes are inserted into pET100/D-TOPO vectors
-
expression of the His-tagged catalytic core of MetRS in Escherichia coli using the expression vector AVA0421
-
into the vector pET101/D-TOPO, a His-Tag is attached, for expression in Escherichia coli BL21 StarDE3 cells
A0R3E2
DNA sequence determination and analysis, overexpression in Escherichia coli
-
expressed as a glutathione S-transferase fusion protein in Escherichia coli
-
DNA and amino acid sequence determination, overexpression of full-length wild-type and a deleted version lacking the C-terminal EMAPII-like domain in Escherichia coli BL21(DE3)
Q9ZTS1
full-length MetRS with an N-terminal His-tag is overexpressed in Escherichia coli
-
MetRS DNA and amino acid sequence analysis, phylogenetic tree
Q181D9
gene metS, expression in Escherichia coli leads to production of 2 thermostable proteins
Q9V011
modified gene metS, expression of M606 enzyme in Escherichia coli
Q9V011
expression of cytoplasmic and mitochondrial isozymes as GST-fusion proteins in the yeast strain RS453, functional complementation of an inactive gene disruption yeast strain by the mitochondrial isozyme located in the cytoplasm
-
expression of wild-type and mutant His-tagged MetRSs in Escherichia coli strain BL21(DE3)
P00958
into an inducible Escherichia expression vector
-
bacterial strains, DH5alpha, containing pPROLar plasmids carrying the gene encoding MetRS1 are used
-
expressed in Escherichia coli BL21(DE3) cells
Q38C91
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A256X
-
random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme, random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
C477S
-
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
D369A
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation and 125fold loss in tRNAMet aminoacylation efficiency compared to the wild-type enzyme
D369A
-
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
D369K/K295D
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
D369N
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation and 60fold loss in tRNAMet aminoacylation efficiency compared to the wild-type enzyme
D666A
-
activity is similar to the wild-type enzyme
F277L
-
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
G23A
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
G23P
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H21N
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H21Q
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H24N
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H24Q
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H301L
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
K295A
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K295V
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K335Q
-
mutants produced by site-directed mutagenesis, Lys335-Gln substitution results in a complete loss of activity, similar loss of activity is observed when Lys335 is changed into alanine, glutamic acid, or arginine
L13G
-
saturation mutagenesis, three mutant clones from screening of a saturation mutagenesis library, the mutants are capable of incorporating the long-chain amino acid azidonorleucine into recombinant proteins with modest efficiency
L13N/Y260L/H301L
-
the mutant enzyme enables cells to use the methionine surrogate azidonorleucine in protein synthesis
L13S
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
L13S/Y260L/H301L
-
MetRS SLL-mutant with modified substrate specifity
L22A
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
M218A
-
random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme, random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M233I
-
random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme, random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M78L
-
random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme, random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
P257X
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
Q211
-
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
Q213A
-
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
T10M
-
natural mutant, 5% activity compared to the wild-type, complementation of an enzyme-deficient Escherichia coli strain, no inhibition by L-methionine hydroxamate
T489A
-
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
W221A
-
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
W461D
-
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
Y15A
-
natural mutant, very low residual activity, complementation of an enzyme-deficient Escherichia coli strain
Y260L
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
Y490A
-
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
F370L
P56192
the mutant has 18% of wild type activity
I523T
P56192
the mutant has 16% of wild type activity
K860A
-
site-directed mutagenesis, reduced activity
K863A
-
site-directed mutagenesis, reduced activity
K866A
-
site-directed mutagenesis, reduced activity
K880A
-
site-directed mutagenesis, altered kinetics
R857A
-
site-directed mutagenesis, reduced activity
S662D
-
the mutation induces a conformational change in methionyl-tRNAsynthetase and significantly reduces its interaction with aminoacyl-tRNA synthetase-interacting multifunctional protein-3. This mutant possesses significantly reduced catalytic activity because of loss of tRNAMet binding, resulting in down-regulation of global translation
D229E
-
spontaneous resistant mutant, first step
D229N
-
serial passage mutant, spontaneous resistant mutant, first step
G213C
-
spontaneous resistant mutant, first step
G213D
-
spontaneous resistant mutant, first step
G54A
-
spontaneous resistant mutant, first step
G54C
-
spontaneous resistant mutant, first step
G54S
-
spontaneous resistant mutant, first step
G54S/L203S
-
spontaneous resistant mutant, second step
H101D
-
spontaneous resistant mutant, first step
H101L
-
spontaneous resistant mutant, first step
H101N
-
spontaneous resistant mutant, first step
H101N/G213C
-
spontaneous resistant mutant, second step
I105M/G213D
-
spontaneous resistant mutant, second step
I57N
-
spontaneous resistant mutant, first step
I57N/H101N
-
spontaneous resistant mutant, second step
T236K
-
spontaneous resistant mutant, first step
V216A
-
spontaneous resistant mutant, first step
V216F/L203S
-
spontaneous resistant mutant, second step
A355C
-
site-directed mutagenesis, 115% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
C337A/C340A
-
site-directed mutagenesis, inactive
C350A
-
site-directed mutagenesis, 1.5% activity compared to the wild-type enzyme, no in vivo complementation of a deficient yeast strain
C350A/C353A
-
site-directed mutagenesis, inactive
C353A
-
site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain
C367A
-
site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain, mutant shows a second zinc-binding knuckle structure
D348G
-
site-directed mutagenesis, 4.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
D370A
-
site-directed mutagenesis, 8.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
G347R
-
site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain
P338I
-
site-directed mutagenesis, 74% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
A247E
-
mutant MetRS
G223C
-
mutant MetRS
G54A/A64P
-
mutant MetRS
G54S
-
mutant MetRS
I57N
-
mutant MetRS
I57N/A247E
-
mutant MetRS
I57N/G54S
-
mutant MetRS
I57N/I238F
-
mutant MetRS
I57N/V242F
-
mutant MetRS
L213W
-
mutant MetRS
V108M
-
mutant MetRS
additional information
-
gene replacement mutagenesis, downregulation of metS1 by its antisense construct, xylose-induced antisense expression, antisense orientation is identified for the metS1 allele, while no such orientation bias is seen for the metS2 allele, attenuation of MetS1 enzyme expression hypersensitizes Bacillus anthracis cells to a MetS-specific antimicrobial compound Rx-000019, but not to other antibiotics that affect cell wall assembly, fatty acid biosynthesis, protein translation, or DNA replication, overview
additional information
-
construction of truncated mutants lacking the tRNA-binding domain, deletion of the C-terminal tRBD of MetRS-Ce results in a 10fold increase in the kcat of Met-tRNAMet formation and a 15fold increase in KM for tRNAMe compared to the wild-type enzyme
M88F
-
random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme, random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
additional information
-
mutant strains with an increased Km for methionine
additional information
-
construction of C-terminal truncated mutant, removal of beta10 strand and insertion of a stop codon at position 666, M665
additional information
-
high-throughput screening for mutant enzymes that enable residue-specific incorporation of noncanonical amino acids into the recombinant mutant enzymes in the bacterial cells, overview
additional information
-
replacement of amino acids of the MetRS SCF with portions of the structurally similar glutaminyl-tRNA synthetase, EC6.1.1.18, motif or with alanine residues. Chimeric variants retain significant tRNA methionylation activity, indicating that structural integrity of the helix-turn-strand-helix motif contributes more to RNA aminoacylation than does amino acid identity. In contrast, chimeras are significantly reduced in methionyl adenylate synthesis, suggesting a role for the SCF in formation of a structured active site domain
Y94H
-
natural mutant, unstable, no complementation of an enzyme-deficient Escherichia coli strain
additional information
Escherichia coli K12
-
mutant strains with an increased Km for methionine
-
additional information
-
construction of a truncated enzyme form with 25% reduced activity compared to the wild-type enzyme
I363N
-
site-directed mutagenesis, 84% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
additional information
-
a strain carrying the MES1 structure gene on a high copy number plasmid, pFL1
additional information
-
construction of an inactive strain by gene disruption
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
facile, after unfolding with 5 M guanidine under conditions where zinc is not sequestred
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
the enzyme is an important antibiotic target
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug
medicine
-
REP8839 is a selective inhibitor of methionyl-tRNA synthetase with antibacterial activity against a variety of gram-positive organisms
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug
medicine
-
REP8839 is a selective inhibitor of methionyl-tRNA synthetase with antibacterial activity against a variety of gram-positive organisms
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug
medicine
-
REP8839 is a selective inhibitor of methionyl-tRNA synthetase with antibacterial activity against a variety of gram-positive organisms
medicine
-
REP3123 is a fully synthetic methionyl-tRNA synthase inhibitor in pre-clinical development as a novel agent to treat Clostridium difficile infection, CDI
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug to combat Clostridium difficile infections
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug
medicine
-
REP8839 is a selective inhibitor of methionyl-tRNA synthetase with antibacterial activity against a variety of gram-positive organisms
medicine
-
REP3123 represents a promising narrow spectrum, new mode-of-action agent with an excellent microbiological profile that warrants its further evaluation as a novel drug
medicine
-
REP8839 is a selective inhibitor of methionyl-tRNA synthetase with antibacterial activity against a variety of gram-positive organisms
drug development
-
parasite MetRS is an attractive drug target due to its essential role in protein synthesis and cell survival. Comparative sequence analysis discloses differences between the trypanosome and mammalian methionyl-tRNA synthetases