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Information on EC 6.1.1.20 - phenylalanine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.20
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EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.20 phenylalanine-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 6.1.1.20
- aminoacylation
- synthetases
- aminoacyl-trna
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phenylalanylation
- thermophilus
- thermus
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anticodon
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aarss
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proofreading
- phe-trnaphe
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noncognate
- tyrosyl-trna
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misacylated
- seryl-trna
- threonyl-trna
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misaminoacylated
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mischarging
- trna-phe
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aminoacyladenylate
- valyl-trna
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alphabeta2
- biotechnology
showSynonyms
phenylalanyl-trna synthetase, phers, fars2, mitochondrial phenylalanyl-trna synthetase, mtphers, mitochondrial phers, phenylalanine trna synthetase, phenylalanine-trna synthetase, ecphers, hcphers, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cFRS
CML33
cytoplasmic phenylalanyl-tRNA synthetase
cytosolic phenylalanine tRNA-synthetase
cytosolic phenylalanyl-tRNA synthetase
FARS2
FRS
hcPheRS
HSPC173
L-Phenylalanyl-tRNA synthetase
mitochondrial phenylalanyl-tRNA synthetase
mitPheRS
mtPheRS
Phe-RS
Phenylalanine translase
phenylalanine tRNA synthetase
Phenylalanine--tRNA ligase
Phenylalanine-tRNA synthetase
Phenylalanyl transfer ribonucleic acid synthetase
phenylalanyl tRNA synthase
phenylalanyl tRNA synthetase
Phenylalanyl-transfer ribonucleate synthetase
Phenylalanyl-transfer RNA ligase
Phenylalanyl-transfer RNA synthetase
Phenylalanyl-tRNA ligase
Phenylalanyl-tRNA synthetase
PheRS
Synthetase, phenylalanyl-transfer ribonucleate
additional information
the enzyme belongs to class II aminoacyl-tRNA synthetases
CML33
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FRS
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-
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HSPC173
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-
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L-Phenylalanyl-tRNA synthetase
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-
-
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L-Phenylalanyl-tRNA synthetase
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Phenylalanine translase
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-
-
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Phenylalanine--tRNA ligase
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-
-
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Phenylalanine-tRNA synthetase
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-
-
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Phenylalanine-tRNA synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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PheRS
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PheRS
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Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
reaction mechanism in which ATP and phenylalanine enter the reaction in an obligatory ordered fashion. A random mechanism is not completely eliminated
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNA channeling mechanism
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
Phe391 in motif 2 and Arg472 in motif 3 bind to the adenosine moiety of tRNAPhe, Arg379 in motif 2 and Arg463 in motif 3 restrain the conformation with the triphosphate that interacts with the ribosyl hydroxyl and gamma-phosphate, Asp395 in motif 2 is unique and binds to phenylalanine to assure proper positioning of the substrate
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNAPhe substrate binding mechanism, base-specific interactions between the 3'-end of the tRNA and the enzymes alpha- and beta-subunit
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
substrate binding mechanism, residues S180, Q218, E220, W149, H178, R204, and Q218 are involved in binding of phenylalanine via hydrogen bonds
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNA recognition and binding mode
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
reaction mechanism
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
mechanism, the reaction intermediate is bound to the active site cleft in the catalytic alpha-subunit
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
two-step reaction, the second reaction step is the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
residue N217 is essential for catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
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-
-
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esterification
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
tRNA charging
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine:tRNAPhe ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9055-66-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
ATP + 2-L-naphthylalanine + tRNAPhe
AMP + diphosphate + 2-L-naphthylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L--tyrosyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L-tyrosyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + 4-acetyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-acetyl-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant T251G, no activity with A294G
Products: -
Products: -
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
ATP + 4-bromo-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-bromo-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant A294G
Products: -
Products: -
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ATP + 4-cyano-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-cyano-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant A294G
Products: -
Products: -
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ATP + 4-ethynyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-ethynyl-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant A294G
Products: -
Products: -
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
ATP + 4-iodo-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-iodo-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant A294G
Products: -
Products: -
?
ATP + benzofuranylalanine + tRNAPhe
AMP + diphosphate + L-benzofuranylalanyl-tRNAPhe
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Substrates: benzofuranylalanine is a substrate for aminoacylation of tRNAPhe by mutant enzyme with mutation A294G in the alpha-subunit
Products: -
Products: -
?
ATP + L-alanine + tRNAPhe
AMP + diphosphate + L-alanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
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Substrates: -
Products: -
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ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-phenylalanine + tRNAPhe-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
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Substrates: tRNAPhe variant, 370fold reduced activity compared to wild-type tRNAPhe
Products: -
Products: -
?
ATP + L-tryptophan + tRNAPhe
AMP + diphosphate + L-tryptophanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-Tyr + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
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Substrates: cytosolic PheRS contains an editing site, which upon disruption abolishes both cis and trans editing of Tyr-tRNAPhe. Wild-type mitochondrial PheRS lacks cis and trans editing and can synthesisze Tyr-tRNAPhe
Products: -
Products: -
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
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Substrates: PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview
Products: -
Products: -
?
GTP + L-phenylalanine + tRNAPhe
GMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: 40fold lower activity compared to ATP
Products: -
Products: -
?
N6-methyladenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
N6-methyladenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
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Substrates: mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging
Products: overcharged product cannot be isolated from living cells
Products: overcharged product cannot be isolated from living cells
ir
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging
Products: overcharged product cannot be isolated from living cells
Products: overcharged product cannot be isolated from living cells
ir
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
-
Substrates: -
Products: -
Products: -
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
Substrates: 0.13% activity compared to L-phenylalanine
Products: -
Products: -
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
Substrates: 0.33% activity compared to L-phenylalanine
Products: -
Products: -
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
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Substrates: recombinant mutant A294G
Products: -
Products: -
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
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Substrates: suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
Products: -
Products: -
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ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
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Substrates: suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
Products: -
Products: -
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ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
Substrates: 1.9% activity compared to L-phenylalanine
Products: -
Products: -
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
Substrates: 22% activity compared to L-phenylalanine
Products: -
Products: -
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
-
Substrates: -
Products: -
Products: -
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: various mutant transcripts of phenylalanine tRNA prepared by an in vitro transcription system are examined. The results indicated that anticodon nucleotides G34, A35 and A36, discriminator base A73 and G20 in the variable pocket are base-specifically recognized by the enzyme
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: various mutant transcripts of phenylalanine tRNA prepared by an in vitro transcription system are examined. The results indicated that anticodon nucleotides G34, A35 and A36, discriminator base A73 and G20 in the variable pocket are base-specifically recognized by the enzyme
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: cognate amino acid charging
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
Products: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: aminoacylates native yeast tRNAPhe
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: activity with mutant yeast tRNAPhe transcripts
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: the N-terminal coiled-coil structure of the alpha-subunit is involved in the binding of cognate tRNAPhe
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: tRNAPhe substrate from Escherichia coli, two-step reaction, the first step, formation of the aminoacyl-adenylate, is reversible, the second, transfer of the activated amino acid to the tRNA, is not
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: charging of cognate amino acid
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: recognition of phenylalanyl-adenylate and substrate binding structure, docking model, overview. Formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement, i.e. hinge-type rotation through about 160degree, of the anticodon binding domain upon tRNA binding, overview
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: 100% activity
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Klebsiella pneumoniae 21856
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: heterologous aminoacylation of tRNA with high selectivity for archaebacterial tRNA
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: tRNAs from E. coli and bean chloroplast are not aminoacylated
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Pseudomonas aeruginosa PAO01
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: editing mechanism of noncognate aminoacyl-tRNA involving domains B3 and B4 and residues Leu202, Ser211, Asp234, and Thr236, overview
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: activity is restricted to endogenous tRNA, highly specific for L-phenylalanine
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: enzyme is essemtial for poly(Phe) synthesis
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: discrimination between phenylalanine and 18 other naturally occuring amino acids, discrimination factors
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: five major recognition nucleotides: G20, G34, A35, A36, and A73. The noncognate tRNAs are missing a sufficient number of recognition nucleotides or have a structure imcompatible for the formation of a complex with phenylalanine-tRNA ligase
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: structure-activity relationship, overview
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: can incorporate more than one molecule of Phe into tRNAPhe. The hyperaminoacylated tRNAPhe is the bis-2',3'-O-phenylalanyl-tRNAPhe
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: mutant tRNAs with substitutions at position 16, 17, 19, or 20 (in the D loop), 34-36 (in the anticodon loop), 26, 44 (at the top of the anticodon stem), 56 (in the T loop), 73 (in the acceptor end) and at the base pairs 10*25 (in the D stem), 27*43 and 28*42 (in the anticodon). Nucleotide 20 and some tertiary nucleotides, including the conserved G19*C56 base pair, are proposed to participate in stabilization of the precise tRNA conformation required for efficient aminoacylation
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: reaction intermediate aminacyl-AMP stucture
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: the recognition of Phe through a mixture of van der Waals interactions and hydrogen bonds
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: two-step reaction, the first step, formation of phenylalanyl-adenylate intermediate, proceeds also within crystals, where the intermediate is bound to the active site involving neighbouring residues Phe258 and Phe260
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: wild-type tRNAPhe substrate, enzyme interacts with the 3'-end of tRNAPhe
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
Products: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: effect of nucleotide replacement in tRNAPhe on positioning of the acceptor end in the complex with phenylalanine-tRNA synthetase
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: charging of cognate amino acid, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP or AMP binding, acceptor arm binding and recognition
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
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Substrates: -
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ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
Substrates: -
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ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
Substrates: 0.089% activity compared to L-phenylalanine
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ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
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Substrates: -
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additional information
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Substrates: enzyme expression, genes pheS and pheT, is regulated by iron availability
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additional information
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Substrates: enzyme expression, genes pheS and pheT, is regulated by iron availability
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additional information
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-
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Substrates: no activity with L-tryptophan
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additional information
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Substrates: ATP-diphosphate exchange
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additional information
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Substrates: a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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additional information
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Substrates: synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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additional information
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Substrates: in vitro selection of small RNAs that bind to E. coli phenylalanyl-tRNA synthetase
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additional information
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Substrates: phenylalanyl-tRNA synthetase misactivates tyrosine and subsequently corrects such errors through hydrolysis of tyrosyl-adenylate and Tyr-tRNAPhe. Editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code
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additional information
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Substrates: PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
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additional information
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Substrates: editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
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additional information
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Substrates: the enzyme also performs the ATP-diphosphate exchange reaction
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additional information
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Substrates: the enzyme also performs the ATP-diphosphate exchange reaction
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additional information
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
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Substrates: the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynaud's disease, and arthralgias, overview
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additional information
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Substrates: ATP-diphosphate exchange
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additional information
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Substrates: a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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additional information
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Substrates: a number of phenylalanine-analogous can replace phenylalanine in ATP-diphosphate exchange: methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-1-ylalanine, 2-amino-4-methylhex-4-enoic acid, ochratoxin A
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additional information
?
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Substrates: synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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additional information
?
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Substrates: ATP-diphosphate exchange
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additional information
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Substrates: a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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additional information
?
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Substrates: synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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additional information
?
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Substrates: editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
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additional information
?
-
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Substrates: ATP-diphosphate exchange
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additional information
?
-
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Substrates: ATP-diphosphate exchange
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additional information
?
-
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Substrates: a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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additional information
?
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Substrates: synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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additional information
?
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Substrates: very low activity with L-DOPA and 4-L-tyrosine
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additional information
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Substrates: phylogenetic analysis
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additional information
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Substrates: no activity with tRNAPhe-s4 U76, a tRNA variant harboring a 4-thiouridine residue in the 3'-end
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additional information
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Substrates: the enzyme interacts with DNA, more efficiently with single-stranded than with double-stranded DNA, the binding site for DNA is located near the interface between the alpha and beta subunits and is distinct from the tRNAPhe binding site
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additional information
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Substrates: the enzyme probably interacts with DNA
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additional information
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Substrates: the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
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additional information
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Substrates: the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
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additional information
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Substrates: the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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additional information
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Substrates: the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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additional information
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Substrates: tRNAPhe binding structure determination: CCA end orientation is stabilized by extensive base-specific interactions of A76 and C75 with the protein and by intra-RNA interactions of A73 with adjacent nucleotides, the 4-amino group of the bulged out C75 is trapped by two negatively charged residues of the beta-subunit, Glubeta31 and Aspbeta33, highly conserved in eubacterial PheRSs, the position of the A76 base is stabilized by interactions with HisR212 of motif 2 (universally conserved in PheRSs) and class II-invariant ArgR321 of motif 3, overview
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additional information
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Substrates: editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
Substrates: PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: cognate amino acid charging
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Klebsiella pneumoniae 21856
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Pseudomonas aeruginosa PAO01
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: enzyme is essemtial for poly(Phe) synthesis
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Substrates: -
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additional information
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Substrates: enzyme expression, genes pheS and pheT, is regulated by iron availability
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additional information
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Substrates: enzyme expression, genes pheS and pheT, is regulated by iron availability
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additional information
?
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Substrates: phenylalanyl-tRNA synthetase misactivates tyrosine and subsequently corrects such errors through hydrolysis of tyrosyl-adenylate and Tyr-tRNAPhe. Editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code
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additional information
?
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Substrates: PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
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additional information
?
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
?
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Substrates: the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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additional information
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Substrates: the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynaud's disease, and arthralgias, overview
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additional information
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Substrates: phylogenetic analysis
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additional information
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Substrates: the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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additional information
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Substrates: the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
mitochondrial isozyme, high concentration is required for maximal activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
not bound to the active site, located at the interface of alpha and beta subunits
spermine
optimal at 1 mM, stimulates 2-4fold the second reaction step, the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
Zn2+
additional information
-
enzyme metal binding site structure, overview
Mg2+
-
the catalytically significant dissociation constant of MgATP and MgP2O7- and their Michaelis-Menten constants vary considerably as a function of the concentration of Mg2+
Mg2+
optimal at 5-10 mM, required, stimulates 2-4fold the second reaction step, the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
Mg2+
-
both MgP2O7- and Mg2P2O7 participate in the pyrophosphorolysis of the aminoacyl adenylate
Zn2+
-
required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
Zn2+
-
influence of Zn2+ on partial reactions of diadenosine 5',5'''-P1,P4-tetraphosphate synthesis
Zn2+
-
required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,3aS,5aR,10R,10aR)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
-
(2R,3R,3aS,5aR,10S,10aR)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
-
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.0026 mM; IC50: 0.0031 mM
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00047 mM; IC50: 0.00051 mM
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00017 mM; IC50: 0.00026 mM
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
-
IC50: 0.011 mM; IC50: 0.033 mM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
(8R,9R,10S)-10-(hydroxymethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
(8R,9S)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
(8R,9S,10S)-10-(aminomethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
(8R,9S,10S)-10-[[acetyl(methyl)amino]methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
([(8R,9R,10R)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)acetic acid
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
1-(4-bromothiophen-2-yl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 50 nM
1-(4-bromothiophen-2-yl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 120 nM
1-(4-bromothiophen-2-yl)-2-[(2-[[4-(methylsulfonyl)benzyl]oxy]benzyl)amino]ethanol
-
IC50: 26 nM
1-(4-bromothiophen-2-yl)-2-[[2-(2-hydroxyethoxy)benzyl]amino]ethanol
-
IC50: 8 nM
1-(4-bromothiophen-2-yl)-2-[[2-(but-3-en-1-yloxy)benzyl]amino]ethanol
-
IC50: 18 nM
1-(4-bromothiophen-2-yl)-2-[[2-(methoxymethoxy)benzyl]amino]ethanol
-
IC50: 35 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-2-ylmethoxy)benzyl]amino]ethanol
-
IC50: 43 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-3-ylmethoxy)benzyl]amino]ethanol
-
IC50: 18 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-4-ylmethoxy)benzyl]amino]ethanol
-
IC50: 16 nM
1-[3-(hydroxymethyl)phenyl]-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 570 nM
1-[3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl]-3-(1,3-thiazol-2-yl)urea
-
binding structure and inhibition mechanism, the inhibitor molecule binds with ring A deep inside the enzyme, and ring B in the place that is occupied by the aromatic ring of phenylalanine, overview
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethoxy)phenyl]ethanol
-
IC50: 190 nM
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 160 nM
2-[(2-methylbenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 790 nM
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]benzoic acid
-
IC50: 2500 nM
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]phenol
-
IC50: 100 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)acetamide
-
IC50: 110 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-ethylacetamide
-
IC50: 32 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetamide
-
IC50: 42 nM
2-[4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butyl]-1H-isoindole-1,3(2H)-dione
-
IC50: 22 nM
2-[[2-(1H-benzimidazol-2-ylmethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 26 nM
2-[[2-(2-aminoethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 220 nM
2-[[2-(4-aminobutoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 22 nM
2-[[2-(benzyloxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 10 nM
2-[[2-(benzyloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 50 nM
2-[[2-(difluoromethoxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 260 nM
2-[[2-(prop-2-en-1-yloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 58 nM
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
3-([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)propanoic acid
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)propanamide
-
IC50: 25 nM
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]propanamide
-
IC50: 36 nM
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]propanoic acid
-
IC50: 58 nM
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)butanamide
-
IC50: 26 nM
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]butanamide
-
IC50: 30 nM
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butanoic acid
-
IC50: 43 nM
Alkylamides of phenylalanine
-
the inhibitor constant decreases with increasing length of the alkyl chain
E. coli tRNAPhe
-
inhibition by formation of a tight complex of the enzyme with the diphosphate formed during the aminoacylation
-
methyl ([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)methylsulfuramidoite
methyl ([(8R,9R,10S)-6-[[4-(cyclopropyloxy)phenyl]carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)methylsulfuramidoite
-
methyl [(8R,9R,10S)-3,4-dihydroxy-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methanesulfinate
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
N-([(8R,9S,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)-beta-alanine
N-benzyl-D-amphetamine
-
most potent competitive inhibitor, selectivity for bacterial enzyme
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
-
IC50: 120 nM
phenyl-thiazolylurea-sulfonamido-aminoethylindole
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
-
IC50: 49 nM
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.002 mM
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.00017 mM
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.0016 mM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 600 nM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 10 nM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 70 nM
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 40 nM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 40 nM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00099 mM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00073 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.004 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.003 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0087 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0061 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00085 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00056 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00022 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00007 mM, high selectivity over the human enzyme
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM, high selectivity over the human enzyme
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 2 nM, high selectivity over the human enzyme
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0083 mM, high selectivity over the human enzyme
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0137 mM, high selectivity over the human enzyme
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.032 mM, high selectivity over the human enzyme
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.045 mM, high selectivity over the human enzyme
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 130 nM
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 4 nM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 820 nM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 3200 nM
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
BRD1389, binds the enzyme selectively and inhibits aminoacylation via L-Phe competition
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
BRD1389, binds the enzyme selectively and inhibits aminoacylation via L-Phe competition
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
BRD1389, binds the enzyme selectively and inhibits aminoacylation via L-Phe competition
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
(8R,9R,10S)-10-(hydroxymethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9R,10S)-10-(hydroxymethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9R,10S)-10-(hydroxymethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
(8R,9S)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-(aminomethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-(aminomethyl)-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
potent and selective inhibitor
(8R,9S,10S)-10-[[acetyl(methyl)amino]methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
(8R,9S,10S)-10-[[acetyl(methyl)amino]methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
-
-
([(8R,9R,10R)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)acetic acid
-
-
([(8R,9R,10R)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)acetic acid
-
-
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
-
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl) ethyl)-1,3,4-thiadiazol-2-yl) amino)-3-(4-chlorophenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(2-methoxy phenyl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxo-3-(p-tolyl)propan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)ethyl)-1,3,4-thiadiazol-2-yl)amino)-3-(naphthalen-2-yl)-1-oxopropan-2-aminium
-
-
1-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)1H-benzimidazole
-
-
1-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)1H-benzimidazole
-
-
1-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)1H-benzimidazole
-
-
1-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-1H-benzimidazole
-
-
1-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-1H-benzimidazole
-
-
1-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-1H-benzimidazole
-
-
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 15 nM
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 15 nM
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 50 nM
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
-
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
-
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
-
-
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
-
-
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
-
-
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
-
-
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
-
-
3-(4-chlorophenyl)-1-((5-(2-(4-(dimethylamino)-7H-pyrrolo[2,3-d] pyrimidin-7-yl) ethyl)-1,3,4-thiadiazol-2-yl)amino)-1-oxopropan-2-aminium
-
-
3-([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)propanoic acid
-
-
3-([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methoxy)propanoic acid
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
-
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
9-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
-
9-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
-
9-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
-
9-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
9-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
9-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
-
-
methyl ([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)methylsulfuramidoite
-
-
methyl ([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)methylsulfuramidoite
-
-
methyl ([(8R,9R,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)methylsulfuramidoite
-
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl [(8R,9R,10S)-3,4-dihydroxy-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methanesulfinate
-
-
methyl [(8R,9R,10S)-3,4-dihydroxy-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methanesulfinate
-
-
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
-
-
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
-
-
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-3,5-dimethoxybenzamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-3,5-dimethoxybenzamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-3,5-dimethoxybenzamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1.3.4-thiadiazol-2-yl)-4fluorobenzamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1.3.4-thiadiazol-2-yl)-4fluorobenzamide
-
-
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1.3.4-thiadiazol-2-yl)-4fluorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-(4-chlorophenyl) methanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-1-phenylmethanesulfonamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-chlorophenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(4-methoxyphenyl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-1-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-(naphthalen-2-yl) acetamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-2-naphthamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-chlorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-chlorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-chlorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-chlorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-chlorobenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-methoxybenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-methoxybenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-methoxybenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-methoxybenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-4-methoxybenzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)benzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)benzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)benzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)benzamide
-
-
N-(5-(2-(1H-benzo[d]imidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)benzamide
-
-
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
N-([(8R,9S,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)-beta-alanine
-
-
N-([(8R,9S,10S)-6-[(4-methoxyphenyl)carbamoyl]-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decan-10-yl]methyl)-beta-alanine
-
-
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 8 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 8 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 50 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
-
-
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
-
-
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
-
-
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
-
-
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
-
-
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
-
-
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
PheOH-AMP
-
L-phenylalaninyl-5'-adenylate, a nonhydrolyzable phenylalanyladenylate analogue, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP binding: the motif 2 loop and a helical loop, residues 139-152 of the alpha-subunit, undergo coordinated displacement, Metalpha148 of the helical loop adopts a conformation preventing the 2'-OH group of A76 from approaching the alpha-carbonyl carbon of PheOH-AMP, the unfavorable position of the terminal ribose stems from the absence of the R-carbonyl oxygen in the analogue, overview
Zn2+
-
inhibition is fully reversible by the addition of zinc-complexing agents
Zn2+
-
inhibition of tRNAPhe aminoacylation, required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
Zn2+
-
inhibition of tRNAPhe aminoacylation, required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
-
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
-
additional information
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynauds disease, and arthralgias, overview
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
Biophysical characterization Of Alpers encephalopathy associated mutants of human mitochondrial phenylalanyl-tRNA synthetase.
Brain Diseases
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Brain Diseases
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Brain Diseases
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
Brain Diseases
FARS2 mutation and epilepsy: Possible link with early-onset epileptic encephalopathy.
Brain Diseases
FARS2 mutations presenting with pure spastic paraplegia and lesions of the dentate nuclei.
Brain Diseases
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Brain Diseases
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Carcinoma, Hepatocellular
A comparison of phenylalanyl-tRNA synthetase from rat liver and a minimal deviation hepatoma.
Carcinoma, Hepatocellular
Effects of ochratoxin A metabolites on yeast phenylalanyl-tRNA synthetase and on the growth and in vivo protein synthesis of hepatoma cells.
Cardiovascular Diseases
Developmental Angiogenesis Requires the Mitochondrial Phenylalanyl-tRNA Synthetase.
Cystic Fibrosis
Improving the phenotype risk score as a scalable approach to identifying patients with Mendelian disease.
Cytochrome-c Oxidase Deficiency
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Diabetes Mellitus
Genetic polymorphisms associated with oxaliplatin-induced peripheral neurotoxicity in Japanese patients with colorectal cancer.
Diffuse Cerebral Sclerosis of Schilder
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Diffuse Cerebral Sclerosis of Schilder
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Drug Resistant Epilepsy
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Drug Resistant Epilepsy
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Dysphonia
FARS2 Causing Complex Hereditary Spastic Paraplegia With Dysphonia: Expanding the Disease Spectrum.
Epilepsies, Myoclonic
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Epilepsy
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Epilepsy
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Epilepsy
FARS2 mutation and epilepsy: Possible link with early-onset epileptic encephalopathy.
Epilepsy
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Epilepsy
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Epilepsy
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Leigh Disease
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells.
Leukemia, Myeloid
Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent.
Malaria
Plasmodium falciparum mitochondria import tRNAs along with an active phenylalanyl-tRNA synthetase.
Mitochondrial Diseases
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Mitochondrial Diseases
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Mitochondrial Diseases
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Mitochondrial Diseases
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Muscle Hypotonia
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Muscle Spasticity
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Myoclonus
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Neoplasms
Contribution of upregulated aminoacyl-tRNA biosynthesis to metabolic dysregulation in gastric cancer.
Neurodegenerative Diseases
A Newly Identified Missense Mutation in FARS2 Causes Autosomal-Recessive Spastic Paraplegia.
Pancreatic Neoplasms
Phenotype risk scores (PheRS) for pancreatic cancer using time-stamped electronic health record data: Discovery and validation in two large biobanks.
Paraplegia
A Newly Identified Missense Mutation in FARS2 Causes Autosomal-Recessive Spastic Paraplegia.
Paraplegia
Biophysical characterization Of Alpers encephalopathy associated mutants of human mitochondrial phenylalanyl-tRNA synthetase.
Paraplegia
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
Paraplegia
FARS2 mutations presenting with pure spastic paraplegia and lesions of the dentate nuclei.
Paraplegia
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
phenylalanine-trna ligase deficiency
Developmental Angiogenesis Requires the Mitochondrial Phenylalanyl-tRNA Synthetase.
phenylalanine-trna ligase deficiency
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
phenylalanine-trna ligase deficiency
FARSA mutations mimic phenylalanyl-tRNA synthetase deficiency caused by FARSB defects.
phenylalanine-trna ligase deficiency
Metabolic stroke-like episode in a child with FARS2 mutation and SARS-CoV-2 positive cerebrospinal fluid.
Seizures
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Seizures
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Spastic Paraplegia, Hereditary
FARS2 Causing Complex Hereditary Spastic Paraplegia With Dysphonia: Expanding the Disease Spectrum.
Status Epilepticus
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Tuberculosis
Re-discovery of PF-3845 as a new chemical scaffold inhibiting phenylalanyl-tRNA synthetase in Mycobacterium tuberculosis.
Tuberculosis
Rediscovery of PF-3845 as a new chemical scaffold inhibiting phenylalanyl-tRNA synthetase in Mycobacterium tuberculosis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
2-L-naphthylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
1.4
L-tryptophan
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.2
2-Chloroadenosine 5'-triphosphate
-
mitochondrial, 3'-deoxyadenosine 5'-triphosphate
0.2
2-Chloroadenosine 5'-triphosphate
-
cytoplasmic, 2'-deoxyadenosine 5'-triphosphate
0.38
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.6
3,4-dihydroxy-L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.65
3,4-dihydroxy-L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
2.5
ATP
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.012
DL-m-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.13
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0225
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
0.0261
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
0.0282
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
0.0312
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
0.0331
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
0.00057
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
0.00084
L-phenylalanine
wild type mitochondrial enzyme, at pH 8.5 and 37°C
0.0017
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0026
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0032
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.033
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
11
L-phenylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
1.9
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0002
tRNAPhe
-
substrate from calf liver, , cytoplasmic, aminoacylation
0.00052
tRNAPhe
-
substrate from calf liver, , mitochondrial, aminoacylation
0.0022
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.0025
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.0027
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli
0.0041
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.018
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
additional information
additional information
-
Km value for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
-
additional information
additional information
-
Km-value for tRNA mutants
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
negative cooperativity exists in the binding of all substrates
-
additional information
additional information
-
kinetics, binding energies in the active conformation
-
additional information
additional information
-
full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview
-
additional information
additional information
-
aminoacylation kinetics with Phe and Tyr
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
2-L-naphthylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.0035
L-tryptophan
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.057
3,4-dihydroxy-L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.16
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.23
3,4-dihydroxy-L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
2.9
ATP
ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37°C
0.052
DL-m-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.65
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.975
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
2.645
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
2.88
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
3 - 6
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
3.12
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
3.3
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
6.08
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
0.005
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
0.0095
L-phenylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.075
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.87
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
1.1
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
1.12
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.033
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.077
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.11
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
0.11
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.78
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.82
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli
additional information
additional information
-
turnover numbers for tRNA mutants
-
additional information
additional information
-
turnover numbers for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
turnover numbers for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
turnover numbers for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
-
additional information
additional information
-
turnover-number of tRNAPheG34A is 10% of wild-type value, turnover-number of tRNAPheG34C/A35U is 31% of wild-type value, turnover-number of tRNAPheA36C is 4.2% of wild-type value, turnover-number of tRNAPheU20A is identical to wild-type value, turnover-number of tRNAPheG44C is 2.1% of wild-type value, turnover-number of tRNAPheG19U/C56G is 1.7% of wild-type value
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15500
2-L-naphthylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
2500
L-tryptophan
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.017
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.095
3,4-dihydroxy-L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.37
3,4-dihydroxy-L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.43
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
4.3
DL-m-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
5
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
8.8
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
28.3
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
270
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
650
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
863
L-phenylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000012 - 0.012
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
0.000067 - 0.0037
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
0.00028 - 0.011
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
0.000011 - 0.00011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
0.00083 - 0.00098
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
0.00015
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
0.0000017 - 0.000126
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
0.0000031 - 0.000087
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
0.0000055 - 0.000081
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
0.0000015 - 0.000036
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
0.0000021 - 0.000053
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
0.0000019 - 0.000079
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
0.0024 - 0.023
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
0.000024 - 0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
0.000043 - 0.000046
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
0.000016 - 0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
0.0000015 - 0.000028
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
0.00003 - 0.00005
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
0.000008 - 0.000065
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
0.0000026 - 0.000081
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
0.00005
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
0.0000027 - 0.00006
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
3.4
L-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0000013 - 0.000028
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
0.00015 - 0.0023
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
0.00084
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0000019 - 0.000012
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
0.0064 - 0.064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
0.000012
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
wild type enzyme, at pH 7.5 and 37°C
0.000025
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
wild type enzyme, at pH 7.5 and 37°C
0.001
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
mutant enzyme L550V, at pH 7.5 and 37°C
0.012
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
wild type enzyme, at pH 7.5 and 37°C
0.000067
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.0037
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.00028
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.011
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.000011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00083
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
at pH 7.5 and 37°
0.00098
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
at pH 7.5 and 37°
0.00036
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.046
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
larger than 0.064
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
larger than 0.064
0.0000017
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000126
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.0000031
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.000087
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
larger than 0.064
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
larger than 0.064
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.000156
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.0000055
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.000081
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.0000015
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.000036
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.0000021
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000053
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.000076
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.0000066
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000095
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000029
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000483
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000022
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000254
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000057
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.000393
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.0000019
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000079
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000014
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.000438
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
larger than 0.064
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
larger than 0.064
0.0024
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.023
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
larger than 0.064
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
larger than 0.064
0.000012
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000097
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000024
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000043
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000046
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000016
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.0000015
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.000028
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.00003
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.00005
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.000008
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000065
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000038
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0013
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0000023
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.000042
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.0000026
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.000081
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.0000027
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.00006
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.0136
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.15
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.0065
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
0.064
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
larger than 0.064
0.0035
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
larger than 0.064
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
larger than 0.064
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
larger than 0.064
0.064
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
larger than 0.064
0.00024
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0022
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0000013
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000028
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.00015
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0023
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0000019
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.000012
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.0064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
0.064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026 - 0.0031
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00047 - 0.00051
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00017 - 0.00026
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.00073 - 0.00099
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.003 - 0.004
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.0061 - 0.0087
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.00056 - 0.00085
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.00007 - 0.00022
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.000002 - 0.000005
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.0083 - 0.0137
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.032 - 0.045
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.000004 - 0.00013
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.011 - 0.033
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
0.00082 - 0.0032
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.000012 - 0.001
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
0.000031 - 0.002108
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
0.0023 - 0.0049
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
0.39
1-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)1H-benzimidazole
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
0.561
1-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-1H-benzimidazole
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
0.00011
1-(3-bromophenyl)-2-[(2-methoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 110 nM
0.000031
1-(3-chlorophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 31 nM
0.000032
1-(3-iodophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 32 nM
0.000083
1-(3-methoxyphenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 83 nM
0.000015 - 0.00005
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
0.00005
1-(4-bromothiophen-2-yl)-2-[(2-methoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 50 nM
0.00012
1-(4-bromothiophen-2-yl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 120 nM
0.000026
1-(4-bromothiophen-2-yl)-2-[(2-[[4-(methylsulfonyl)benzyl]oxy]benzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 26 nM
0.000008
1-(4-bromothiophen-2-yl)-2-[[2-(2-hydroxyethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 8 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(but-3-en-1-yloxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 18 nM
0.000035
1-(4-bromothiophen-2-yl)-2-[[2-(methoxymethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 35 nM
0.000043
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-2-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 43 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-3-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 18 nM
0.000016
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-4-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 16 nM
0.00057
1-[3-(hydroxymethyl)phenyl]-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 570 nM
0.00011
2-[(2-methoxybenzyl)amino]-1-(3-methylphenyl)ethanol
Staphylococcus aureus
-
IC50: 110 nM
0.00019
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethoxy)phenyl]ethanol
Staphylococcus aureus
-
IC50: 190 nM
0.00016
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 160 nM
0.00079
2-[(2-methylbenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 790 nM
0.00019 - 0.026
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
0.0025
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]benzoic acid
Staphylococcus aureus
-
IC50: 2500 nM
0.0001
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]phenol
Staphylococcus aureus
-
IC50: 100 nM
0.00011
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)acetamide
Staphylococcus aureus
-
IC50: 110 nM
0.000032
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-ethylacetamide
Staphylococcus aureus
-
IC50: 32 nM
0.000042
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetamide
Staphylococcus aureus
-
IC50: 42 nM
0.0001 - 0.034
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
0.000022
2-[4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butyl]-1H-isoindole-1,3(2H)-dione
Staphylococcus aureus
-
IC50: 22 nM
0.000026
2-[[2-(1H-benzimidazol-2-ylmethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 26 nM
0.00022
2-[[2-(2-aminoethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 220 nM
0.000022
2-[[2-(4-aminobutoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 22 nM
0.00001
2-[[2-(benzyloxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 10 nM
0.00005
2-[[2-(benzyloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 50 nM
0.00026
2-[[2-(difluoromethoxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 260 nM
0.000058
2-[[2-(prop-2-en-1-yloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 58 nM
0.000025
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)propanamide
Staphylococcus aureus
-
IC50: 25 nM
0.000036
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]propanamide
Staphylococcus aureus
-
IC50: 36 nM
0.000058
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]propanoic acid
Staphylococcus aureus
-
IC50: 58 nM
0.000026
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)butanamide
Staphylococcus aureus
-
IC50: 26 nM
0.00003
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]butanamide
Staphylococcus aureus
-
IC50: 30 nM
0.000043
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butanoic acid
Staphylococcus aureus
-
IC50: 43 nM
0.686
9-(3-(4-phenyl-5-(propylthio)-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
-
0.619
9-(3-(5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-yl)propyl)-9H-purin-6-amine
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
0.0014 - 0.08
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
0.345
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1,3,4-thiadiazol-2-yl)-3,5-dimethoxybenzamide
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
0.685
N-(5-(2-(1H-benzimidazol-1-yl)ethyl)-1.3.4-thiadiazol-2-yl)-4fluorobenzamide
Klebsiella pneumoniae
-
at pH 7.5 and 37°C
0.000008 - 0.00005
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
0.0000022 - 0.000013
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
0.00007 - 0.0042
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
0.0000027 - 0.000022
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
0.00012
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
Staphylococcus aureus
-
IC50: 120 nM
0.000049
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
Staphylococcus aureus
-
IC50: 49 nM
0.0026
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.0026 mM
0.0031
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.0031 mM
0.00047
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00047 mM
0.00051
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00051 mM
0.00017
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00017 mM
0.00026
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00026 mM
0.00017
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Escherichia coli
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.00017 mM
0.0016
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Staphylococcus aureus
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.0016 mM
0.002
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Enterococcus faecalis
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.002 mM
0.00001
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Escherichia coli
-
IC50: 10 nM
0.00007
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Staphylococcus aureus
-
IC50: 70 nM
0.0006
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Enterococcus faecalis
-
IC50: 600 nM
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 40 nM, high selectivity over the human enzyme
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 40 nM, high selectivity over the human enzyme
0.00073
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.00073 mM, high selectivity over the human enzyme
0.00099
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.00099 mM, high selectivity over the human enzyme
0.003
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.003 mM, high selectivity over the human enzyme
0.004
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.004 mM, high selectivity over the human enzyme
0.0061
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.0061 mM, high selectivity over the human enzyme
0.0087
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.0087 mM, high selectivity over the human enzyme
0.00056
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.00056 mM, high selectivity over the human enzyme
0.00085
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.00085 mM, high selectivity over the human enzyme
0.00007
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.00007 mM, high selectivity over the human enzyme
0.00022
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.00022 mM, high selectivity over the human enzyme
0.000002
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 2 nM, high selectivity over the human enzyme
0.000005
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 5 nM, high selectivity over the human enzyme
0.0083
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.0083 mM, high selectivity over the human enzyme
0.0137
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.0137 mM, high selectivity over the human enzyme
0.032
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.032 mM, high selectivity over the human enzyme
0.045
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.045 mM, high selectivity over the human enzyme
0.000004
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 4 nM
0.000005
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 5 nM
0.00013
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Escherichia coli
-
IC50: 130 nM
0.011
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
Enterococcus faecalis
-
IC50: 0.011 mM
0.033
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
Enterococcus faecalis
-
IC50: 0.033 mM
0.00082
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 820 nM
0.0032
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Escherichia coli
-
IC50: 3200 nM
0.000012
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Plasmodium falciparum
wild type enzyme, at pH 7.5 and 37°C
0.001
(3S,4R,8R,9R,10S)-N-[4-(cyclopropyloxy)phenyl]-3,4-dihydroxy-10-(methoxymethyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Plasmodium falciparum
mutant enzyme L550V, at pH 7.5 and 37°C
0.000031
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
wild type enzyme, at pH 7.5 and 37°C
0.000135
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
mutant enzyme M484I, at pH 7.5 and 37°C
0.000197
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
mutant enzyme V262A/M484I, at pH 7.5 and 37°C
0.000207
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
mutant enzyme V262A, at pH 7.5 and 37°C
0.001315
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
mutant enzyme L497I, at pH 7.5 and 37°C
0.002108
(8R,9S,10S)-10-[(dimethylamino)methyl]-N-(4-methoxyphenyl)-9-[4-(phenylethynyl)phenyl]-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
Toxoplasma gondii
mutant enzyme L497V, at pH 7.5 and 37°C
0.0023
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
Pseudomonas aeruginosa
-
at pH 7.5 and 37°
0.0049
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
Streptococcus pneumoniae
-
at pH 7.5 and 37°
0.000015
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Haemophilus influenzae
-
IC50: 15 nM
0.000015
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Escherichia coli
-
IC50: 15 nM
0.00005
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Streptococcus pneumoniae
-
IC50: 50 nM
0.016
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
Escherichia coli
-
pH and temperature not specified in the publication
0.2
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
Pseudomonas aeruginosa
-
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.00019
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.026
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0001
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.013
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0001
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.034
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0014
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.082
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00056
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.041
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00006
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
Escherichia coli
-
pH and temperature not specified in the publication
0.01
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.001
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Escherichia coli
-
pH and temperature not specified in the publication
0.059
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00008
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Escherichia coli
-
pH and temperature not specified in the publication
0.011
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0014
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.08
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.000008
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Haemophilus influenzae
-
IC50: 8 nM
0.000008
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Escherichia coli
-
IC50: 8 nM
0.00005
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Staphylococcus aureus
-
IC50: 50 nM
0.0000022
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
Escherichia coli
-
pH and temperature not specified in the publication
0.000013
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00007
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0042
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0000027
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
Escherichia coli
-
pH and temperature not specified in the publication
0.000022
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.2
7.5
8.5
6.5
-
2-(morpholino)ethanesulfonic acid buffer or 2-(2-hydroxy-1,1-bis(hydroxymethyl)ethyl)aminoethanesulfonic acid buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
no activity below pH 6.0 and above 8.5, higher activity range is pH 6.5-8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 90
-
55°C: about 50% of maximal activity, 90°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9Y9I6: alpha-subunit, Q9Y9I3: beta-subunit
SwissProt
brenda
mutant strain UA22 carrying both wild-type and mutant alleles of gene pheS due to polyploidy
UniProt
brenda
carrying the thermosensitive point mutation A294G in the active site
-
-
brenda
i.e. Lactobacillus amylovorus, several strains, e.g. strains 16698T and AD5, from Finnish porcine isolates, housekeeping gene pheS encoding the alpha-subunit
-
-
brenda
-
-
-
brenda
-
285, 310, 322, 323, 326, 330, 333, 336, 337, 340, 342, 344, 351, 651585, 668395, 668401, 669223, 677104, 694872, 706561
-
-
brenda
carrying the thermosensitive point mutation A294G in the active site
-
-
brenda
overproducing strain carrying a hybrid pBR322 plasmid containing the pheS-pheT locus
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
chronic myelogenous leukemic cell line, high content
brenda
colorectal adenocarcinoma cell line, high content
brenda
additional information
additional information
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
brenda
additional information
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
brenda
additional information
-
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
architecture of four helix-bundle interface, characteristic of class IIc heterotetrameric aaRSs, is changed, each of the two long helices belonging to CLM transformed into the coil-short helix structural fragments. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain
malfunction
metabolism
-
elevated enzyme levels induce cell fate changes and tumorous phenotypes in Drosophila midguts. Elevated enzyme levels attenuate Notch signaling when Notch induces differentiation into enterocytes, type II neuroblast stem cell proliferation, or transcription of a Notch reporter
physiological function
malfunction
-
mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency
malfunction
pathogenic variants of the FARS2 gene, encoding the human mitochondrial phenylalanine-tRNA synthetase lead to spastic paraplegia or fatal infantile Alpers encephalopathy
malfunction
-
enzyme knock-down hampers the embryonic development in zebrafish and delays the formation of the vasculature. Enzyme silencing impairs cell motility, proliferation, migration, and tube formation and causes mitochondrial dysfunction in HUVEC cells
physiological function
cytosolic phenylalanyl-tRNA synthetase exerts control over the translation accuracy, hydrolyzing misacylated products, while the monomeric mitochondrial enzyme lacks the editing activity
Show AA Sequence and Transmembrane Helices (58384 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
260000
270000
40000
45000
48000
49600
55000
56000
-
2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
57000
57600
x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
59000
60000
63000
64000
-
2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
66000
66200
x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
70000
72000
90000
-
2 * 40000, alpha subunit, + 2 * 90000, beta-subunit, (alphabeta)2, recombinant enzyme, SDS-PAGE
48000
recombinant mitochondrial isozyme, analytical velocity sedimentation centrifugation
49600
recombinant mitochondrial isozyme, amino acid sequence determination
55000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
55000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
57000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
57000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
57000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
59000
-
2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
60000
Methanobacterium thermoautotrophicus
-
2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
66000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
70000
-
2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
70000
Methanobacterium thermoautotrophicus
-
2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
heterotetramer
monomer
oligomer
tetramer
additional information
?
x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
heterotetramer
-
EcPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
heterotetramer
EcPheRS is a (alphabeta)2 heterotetramer, built of two alphabeta heterodimers
heterotetramer
-
ctPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
monomer
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
oligomer
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
oligomer
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
-
tetramer
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
Methanobacterium thermoautotrophicus
-
2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
tetramer
-
2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
tetramer
-
PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview
tetramer
-
2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
-
2 * 40000, alpha subunit, + 2 * 90000, beta-subunit, (alphabeta)2, recombinant enzyme, SDS-PAGE
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
all forms of homologous subunits have no catalytic activity
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
-
the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
additional information
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
-
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
-
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
-
additional information
-
the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
-
additional information
-
enzyme is part of an aminoacyl-tRNA synthetase complex which is resistant to dissociation when subjected to gel filtration
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
-
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
-
human mitPheRS is a chimera of the bacterial beta-subunit of PheRS and the B8 domain of its beta-subunit, together, the beta-subunit and the RNP-domain, i.e. B8 domain, at the C-terminus form the minimal structural set to construct an enzyme with phenylalanylation activity, overview
additional information
-
human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview
additional information
-
structure molecular dynamics simulations of hmtPheRS, wild-type and mutant enzymes, overview
additional information
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
-
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
-
the amino terminal part of each beta-subunit represents the main tRNA binding domain and is not involved in either catalysis or subunit interactions. The trypsin resistant alpha2beta2 core contains the catalytic site as well as contact areas between subunits
additional information
-
structure analysis and structure-activity relationship, overview
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
all forms of homologous subunits have no catalytic activity
additional information
-
both alpha- and beta-subunits mainly exist in the dimeric form
additional information
-
alphabeta organization, the alpha-subunit is the catalytically active one
additional information
the enzyme is modularly composed of several different domains
additional information
-
the enzyme is modularly composed of several different domains
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
-
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
both alpha- and beta-subunits mainly exist in the dimeric form
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the large subunit of the mitochondrial enzyme is a glycoprotein with nearly 3% carbohydrate by weight. The carbohydrates present are: glucose, N-acetylglucosamine, mannose, galactose and N-acetylneuraminic acid
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and SeMet-labeled PheRs in complex with phenylalanine and AMP, hanging-drop vapor-diffusion method, 20°C using 0.004 ml of protein solution, containing 10 mg/ml protein and 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 1 mM EDTA, 1 mM MgCl2, 10% glycerol, 1 mM Phe and 1 mM ATP, are mixed at 1:1 ratio with precipitant containing 17-20% PEG 8000K, 0.2 M MgCl2, 0.1 M Tris-HCl buffer, pH 8.5, 3% 1,6 hexandiol, and 3% D-galactose, 3 days, mother-liquor solution containing 20% v/v ethylene-glycol, X-ray diffraction structure determination and analysis at 3.05 A resolution
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
purified recombinant mitPheRS in complex with L-phenylalanine and ATP, hanging or sitting drop vapour diffusion method, 0.001-0.003 ml of protein solution containing 6 mg/ml protein in 20 mM Tris-HCl pH 8.0, 100 mM NaCl, 7 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM EDTA and 0.0065% NaN3, is mixed with an equal volume of reservoir solution containing 25 mM Tris-HCl pH 8.5, 10 mM MgCl2, 5 mM ATP, 2 mM L-phenylalanine, equilibration against reservoir solution, at 4°C or 19°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
the structure of cytosolic phenylalanyl-tRNA synthetase in complex with phenylalanine is solved to 3.3 A resolution
the structure of human cytoplasmic phenylalanyl-tRNA synthetase is determined to a resolution of 3.3 A
enzyme in complex with inhibitor BRD1389, hanging drop vapor diffusion method, using 0.1M sodium cacodylate (pH 6.5), 3% (w/v) poly-gamma-glutamic acid (Na+ form, low molecular weight), 3% (w/v) PEG20000, 0.1 M ammonium sulfate, 0.3 M sodium formate
purified recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit, 0.001 ml of protein solution containing 36 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl, mixed with 0.001 ml of precipitant solution, containing 100 mM sodium citrate, pH 5.6, and 16.5% PEG 20000, covarage with a 1:1 mixture of paraffin oil and silicone, 20°C, 1 week, soaking in a soaked in a cryoprotectant solution containing 100 mM sodium citrate, pH 5.6, 18.2% PEG 20000, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
native enzyme crystals are of poor quality diffracting only to 3-5 A resolution, engineered mutant enzymes diffracts to 2.0 A resolution, X-ray diffraction structure determination and analysis, overview
-
crystal structure of complexes of enzyme with L-Tyr, p-chlorophenylalanine, and L-tyrosyl-adenylate
-
enzyme complexed with phenylalanine or the phenylalanyl-adenylate analogue phenylalaninyl-adenylate, X-ray diffraction structure determination at 2.7 and 2.5 A resolution, respectively, and analysis
-
native enzyme complexed with phenylalanyl-adenylate in presence of manganese, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
PheRS in complex with with cognate tRNAPhe and nonhydrolyzable phenylalanyladenylate analogue PheOH-AMP, hanging-drop vapor-diffusion method, 4°C, 3-5 mg/ml protein ina ratio of 1:2,5 with tRNAPhe in 20 mM imidazole-HCl, pH 7.8, 1 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM NaN3, 10% saturated ammonium sulfate, and 1 mM PheOH-AMP, slow equilibration against a reservoir solution containing the crystallization buffer and 27% saturated ammonium sulfate, cryoprotection by 30% v/v glycerol, X-ray diffraction structure determination and anaylsis at 3.1 A resolution, modeling
-
enzyme in complex with inhibitor BRD1389, hanging drop vapor diffusion method, using 0.1M sodium cacodylate (pH 6.5), 3% (w/v) poly-gamma-glutamic acid (Na+ form, low molecular weight), 3% (w/v) PEG20000, 0.1 M ammonium sulfate, 0.3 M sodium formate
enzyme in complex with inhibitor BRD1389, hanging drop vapor diffusion method, using 0.1M sodium cacodylate (pH 6.5), 3% (w/v) poly-gamma-glutamic acid (Na+ form, low molecular weight), 3% (w/v) PEG20000, 0.1 M ammonium sulfate, 0.3 M sodium formate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A450G
L482V
A249G/A356W
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit, kcat/Km is 6.6% of wild-type value
A249G/E334A
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit, kcat/Km is 60% of wild-type value
A249G/H265A
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit, kcat/Km is 52% of wild-type value
A249G/H265L
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit, kcat/Km is 63% of wild-type value
A249G/T354W
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit, kcat/Km is 26% of wild-type value
A293X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
A294G
A294S
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
A295X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
T251G
-
constructed mutant shows relaxed substrate specificity, efficient incorporation of p-acetylphenylalanine and reactive aryl ketones into protein in the Escherichia coli host
A294G
alphaDELTA1-175
truncated N-terminal domain of the alpha subunit of hcPheRS
alphaDELTA60-170
truncated N-terminal domain of the alpha subunit of hcPheRS
D325Y
-
the mutation is associated with early-onset epilepsy and isolated complex IV deficiency in muscle. The mutant is unable to bind ATP and shows consequently undetectable aminoacylation activity
K33C/T351C
mutant, crosslinked catalytic and RNA-binding domains, results in a closed form of mtPheRS that still catalyses ATP-dependent Phe activation, but is no longer able to transfer Phe to tRNA and complete the aminoacylation reaction
N280S
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C/N280S
-
Ser57 and Asn280 map to positions away from the catalytic center and the anticodon binding domain of hmtPheRS, the mutant does not show significant loss in secondary structure or aminoacylation activity in vitro compared to wild-type enzyme. The S57C/N280S double mutant had remarkable stability even at low pH
D286R
-
the mutant shows improvement of activity over the parental enzyme
H283T/P284S/M285D/D286V
-
the mutant shows approximate 8fold improvement of activity over the parental enzyme
P258A/F261P/H283L/M285F/D286Y
-
the mutant shows improvement of activity over the parental enzyme
P284V/D286R
-
the mutant shows improvement of activity over the parental enzyme
A141W
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity
D234A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
E127A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
E219A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
F145A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
I216A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
L168A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
L202A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
L210A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
N217A
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity and shows abolished Tyr-tRNAPhe deacylation activity
Q126A
site-directed mutagenesis, the mutant shows reduced Tyr-tRNAPhe deacylation activity
R137A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
R223A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
S211A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
T221A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
T236A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
Y189A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
N412G/T415G/S418C/S437F
-
the mutant prefers 2-L-naphthylalanine as substrate
T415G
-
the variant shows 10-fold higher activation activity toward Trp than 2-L-naphthylalanine
G318W
-
the variant has a 7.5fold reduction in proofreading due to the prevention of Tyr-tRNAPhe binding in the editing site
V262A7M484I
the mutation confers resistance toward inhibitor BRD7929
additional information
A450G
-
mutation in subunit alpha, tRNAPhe substrate specificity and flexibilty in charging pPhe variants compared to the wild-type enzyme
A294G
-
mutation of the catalytical alpha-subunit, constructed mutant shows relaxed substrate specificity, efficient incorporation of p-iodo, p-ethynyl-, p-cyano-, and p-azidophenylalanines, but not p-acetylphenylalanine, into protein in the Escherichia coli host
A294G
-
mutant enzyme with A294G mutation in alpha-subunit, kcat/Km is 58% of wild-type value
A294G
-
thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
A294G
-
thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
-
additional information
-
engineering of a mutated counter-selectable marker based on the Burkholderia pseudomallei PheS, i.e. the alpha-subunit of PheRS protein, effectiveness in three different transformed Burkholderia species, the mutant PheS protein effectively killed 100% of the bacteria in the presence of 0.1% 4-chlorophenylalanine, overview. Assembling of mutant pheS on several allelic replacement vectors, in addition to construction of selectable markers based on tellurite and trimethoprim resistance that are excisable by flanking unique FLP recombination target sequences, overview
additional information
-
construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
additional information
-
editing-defective PheRS variants display significantly increased tyrosylation levels in the presence of EF-Tu, likely through elongation factor Tu, EF-Tu, protection of synthesized Tyr-tRNAPhe from hydrolysis, overview
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
additional information
-
construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
-
additional information
-
the N-terminal His-tag does not influence the kinetic parameters of tRNAPhe aminoacylation, cleavage of the His-tag by thrombin leads to nonspecific splitting of the enzyme that occurs in parallel to the main reaction
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
additional information
-
construction of enzyme mutants with better crystallization abilities, e.g. a PheRS variant which has both domains I and IV removed, or PheRS surface mutants, overview
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5 - 8
-
high stability of wild-type and mutant mtPheRSs in the pH range, unfolding parameters, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
additional information
-
preincubation with ATP stabilizes against thermal inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is reversibly inactivated under oxidative stress by formation of intra-molecular disulfide bridge which hinders tRNAPhe binding of the enzyme
-
766232
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified recombinant His-tagged mitochondrial isozyme, 50 mM Tris-HCl, pH 7.6, 50 mM KCl, 10 mM MgCl2, 7 mM 2-mercaptoethanol, 10% v/v glycerol, small aliquots, stable for at least 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation is followed by four chromatography columns, anion exchange on a DEAE-Sepharose column, a heparin-Sepharose column, concentrating the protein on a TSK hydrophobic interaction column and finally gel filtration on a column of superfine Sephadex G-200
ammonium sulfate precipitation, Ni-NTA column chromatography, and Superdex 200 gel filtration
His6-tagged proteins are purified on nickel-nitrilotriacetic acid-agarose
HiTrap Ni2+ chelating column chromatography, Ni-NTA column chromatography and Sephacryl S300 gel filtration
mature mitPheRS in Escherichia coli by streptomycin precipitation, ultrafiltration, anion exchange chromatography and heparin affinity chromatography, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
native enzyme from Oxford strain, 50% purity, recombinant enzyme overexpressed in Escherichia coli, over 90% purity
-
Ni-NTA column chromatography
Ni-NTA column chromatography, heparin column chromatography, and Superdex 200 gel filtration
recombinant alpha- and beta-subunit both expressed in Escherichia coli
recombinant His-tagged heterodimers and nontagged subunits from Escherichia coli, over 200fold
-
recombinant His-tagged proteins from Escherichia coli strain M15 by nickel affinity chromatography, complex formation of the two subunits during purification
-
recombinant N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain B834(DE3) by anion exchange chromatography, adsorption chromatography, and gel filtration
His6-tagged proteins are purified on nickel-nitrilotriacetic acid-agarose
-
HiTrap Ni2+ chelating column chromatography, Ni-NTA column chromatography and Sephacryl S300 gel filtration
-
HiTrap Ni2+ chelating column chromatography, Ni-NTA column chromatography and Sephacryl S300 gel filtration
-
Ni-NTA column chromatography, heparin column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, heparin column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
complementatiom of a growth mutant defective in phenylalanylation in vivo by wild-type full-length PheRS from Saccharomyces cerevisiae, the full-length Escherichia coli enzyme A294G, and the truncated mutant PheRSDELTAB2, overexpression of full-length mutant A294G and truncated mutant PheRSDELTAB2A294G in strain XL-1 Blue
-
DNA and amino acid sequence determination of the alpha- and beta-subunit and analysis, expression in COS-7 cells
DNA and amino acid sequence determination, individual cloning and coexpression of His-tagged alpha- and beta-subunits in Escherichia coli resulting in 3 different types of (alphabeta)2 heterodimers with the His-tag at the N-terminus, N-terminally His-tagged beta-subunit renders the enzyme inactive, overexpression of nontagged alpha- and beta-subunits in Escherichia coli
-
Escherichia coli BL21-RIL/pET16b produces His6-tagged mtPheRS encoded by the MSF1 gene, the ctPheRS alpha and beta subunits, encoded by the FRS1 and FRS2 genes, respectively, are expressed in tandem from pQE31-FRS-sc in Escherichia coli BL21-RIL cells
-
Escherichia coli pET21c+ encoding human mtPheRS, FARS2, produces mature His6-tagged wild-type PheRS
-
Escherichia coli strain BL21(pArgU218)/pET21c-PheRS expresses C-terminal His6-tagged mtPheRS, RosettaDE3 cells containing pRARE plasmids encoding tRNAs for rare codons are transformed with the mutant mtPheRS plasmid constructs
expressed in Escherichia coli B834 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta 2(DE3) cells
expression of genes pheS and pheT with an iron-repressible luxAB-reporter activity, which is promotorless due to mutagenic modification, expression is repressed under iron-sufficient conditions and derepressed under iron-limited conditions
expression of N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain B834(DE3)
expression of wild-type and mutant pheS, alpha-subunit encoding, gene in different Burkholderia species, e.g. Burkholderia thailandensis, allelic replacement
-
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Eed-IYRS, overview
-
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ped-IYRS, overview
-
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ted-IYRS, overview
-
genes encoding alpha- and beta-subunit, DNA and amino acid sequence determination and analysis, expression of alpha-subunit and of beta-subunit in Escherichia coli
genes pheS and pheT encoding the alpha and beta subunits in one transcriptional operon, DNA and amino acid sequence determination and analysis, overexpression of both genes in an artificial operon in Escherichia coli
-
mature mitPheRS in Escherichia coli without His-tag, which causes oligomerization of the recombinant enzyme during purification
-
mitochondrial isozyme, DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme
pheS, DNA and amino acid sequence determination and analysis, phylogenetic analysis by multilocus sequence analysis, overview
-
the two subunits of hcPheRS are cloned into two different plasmids, the alpha subunit, residues 1-508, into the vector pET21b+, the beta-subunit, residues 1-589, into pET28b+, for expression in Escherichia coli BLRDE3 cells, no affinity tag is used
two genes encoding subunits alpha and beta, DNA and amino acid sequence determination and analysis, expression as His-tagged proteins in Escherichia coli strain M15
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
design of an enzyme variant which incorporates aryl ketones into proteins
biotechnology
-
misacylation of suppressor tRNAPhe CUA by the PheRS mutant A294G with 4-iodo-L-phenylalanine might be useful in application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins, used for cell-free protein synthesis as a stoichiometric reagent, overview
biotechnology
-
misacylation of suppressor tRNAPhe CUA by the PheRS mutant A294G with 4-iodo-L-phenylalanine might be useful in application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins, used for cell-free protein synthesis as a stoichiometric reagent, overview
-
EXTERNAL LINKS (specific for EC-Number 6.1.1.20)
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Release 2026.1 (March 2026)
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