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Information on EC 6.1.1.20 - phenylalanine-tRNA ligase
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EC Tree
6.1.1.20 phenylalanine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.20
- aminoacylation
- synthetases
- aminoacyl-trna
-
phenylalanylation
- thermophilus
-
anticodon
- thermus
-
aarss
-
phe-trnaphe
-
3'-terminal
-
proofreading
-
misaminoacylated
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alphabeta2
- trna-phe
-
aminoacyladenylate
-
mischarging
- valyl-trna
-
misacylated
- threonyl-trna
-
non-cognate
- seryl-trna
- tyrosyl-trna
-
valylation
- trnatyr
- p-fluorophenylalanine
- biotechnology
- phe-trna
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
CML33, ctPheRS, cytoplasmic phenylalanyl-tRNA synthetase, cytosolic phenylalanyl-tRNA synthetase, cytosolic PheRS, EcPheRS, FARS2, FRS, hcPheRS, HSPC173, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CML33
cytoplasmic phenylalanyl-tRNA synthetase
cytosolic phenylalanyl-tRNA synthetase
FARS2
FRS
hcPheRS
HSPC173
L-Phenylalanyl-tRNA synthetase
mtPheRS
Phe-RS
Phenylalanine translase
Phenylalanine--tRNA ligase
Phenylalanine-tRNA synthetase
Phenylalanyl transfer ribonucleic acid 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
C9QTZ3
the enzyme belongs to class II aminoacyl-tRNA synthetases
CML33
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-
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FRS
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HSPC173
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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Phenylalanine translase
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Phenylalanine--tRNA ligase
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Phenylalanine-tRNA synthetase
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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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Synthetase, phenylalanyl-transfer ribonucleate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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
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ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
reaction mechanism
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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
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
tRNA channeling mechanism
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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
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
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
residue N217 is essential for catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
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esterification
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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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-
-
-
?
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L-tyrosyl-tRNAPhe
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-
-
-
?
ATP + 4-acetyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-acetyl-L-phenylalanyl-tRNAPhe
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recombinant mutant T251G, no activity with A294G
-
?
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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recombinant mutant A294G
-
?
ATP + 4-cyano-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-cyano-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + 4-ethynyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-ethynyl-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
-
?
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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recombinant mutant A294G
-
?
ATP + benzofuranylalanine + tRNAPhe
AMP + diphosphate + L-benzofuranylalanyl-tRNAPhe
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benzofuranylalanine is a substrate for aminoacylation of tRNAPhe by mutant enzyme with mutation A294G in the alpha-subunit
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?
ATP + L-alanine + tRNAPhe
AMP + diphosphate + L-alanyl-tRNAPhe
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?
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
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?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
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?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
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?
ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
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tRNAPhe variant, 370fold reduced activity compared to wild-type tRNAPhe
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?
ATP + L-tryptophan + tRNAPhe
AMP + diphosphate + L-tryptophanyl-tRNAPhe
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-
-
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?
ATP + L-Tyr + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
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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
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?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
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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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?
GTP + L-phenylalanine + tRNAPhe
GMP + diphosphate + L-phenylalanyl-tRNAPhe
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40fold lower activity compared to ATP
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?
N6-methyladenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
N6-methyladenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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-
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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-
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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-
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
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3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
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-
-
-
?
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
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?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
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0.13% activity compared to L-phenylalanine
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?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
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0.33% activity compared to L-phenylalanine
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-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
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?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
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suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
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?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
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suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
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?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
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1.9% activity compared to L-phenylalanine
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-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
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22% activity compared to L-phenylalanine
-
-
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
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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 modofoed nucleotides is not necessary for tRNAPhe overcharging
overcharged product cannot be isolated from living cells
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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 modofoed nucleotides is not necessary for tRNAPhe overcharging
overcharged product cannot be isolated from living cells
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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
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-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
aminoacylates native yeast tRNAPhe
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
activity with mutant yeast tRNAPhe transcripts
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
100% activity
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the N-terminal coiled-coil structure of the alpha-subunit is involved in the binding of cognate tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
charging of cognate amino acid
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
heterologous aminoacylation of tRNA with high selectivity for archaebacterial tRNA
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
tRNAs from E. coli and bean chloroplast are not aminoacylated
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Pseudomonas aeruginosa PAO01
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
editing mechanism of noncognate aminoacyl-tRNA involving domains B3 and B4 and residues Leu202, Ser211, Asp234, and Thr236, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
activity is restricted to endogenous tRNA, highly specific for L-phenylalanine
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
discrimination between phenylalanine and 18 other naturally occuring amino acids, discrimination factors
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
structure-activity relationship, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
can incorporate more than one molecule of Phe into tRNAPhe. The hyperaminoacylated tRNAPhe is the bis-2',3'-O-phenylalanyl-tRNAPhe
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
reaction intermediate aminacyl-AMP stucture
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the recognition of Phe through a mixture of van der Waals interactions and hydrogen bonds
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
wild-type tRNAPhe substrate, enzyme interacts with the 3'-end of tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
effect of nucleotide replacement in tRNAPhe on positioning of the acceptor end in the complex with phenylalanine-tRNA synthetase
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
-
ir
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
0.089% activity compared to L-phenylalanine
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
-
-
-
?
additional information
?
-
-
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
-
additional information
?
-
-
in vitro selection of small RNAs that bind to E. coli phenylalanyl-tRNA synthetase
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
-
-
-
additional information
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
-
-
-
additional information
?
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
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 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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
-
additional information
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
-
additional information
?
-
-
very low activity with L-DOPA and 4-L-tyrosine
-
-
-
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
no activity with tRNAPhe-s4 U76, a tRNA variant harboring a 4-thiouridine residue in the 3'-end
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme probably interacts with DNA
-
?
additional information
?
-
the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
-
?
additional information
?
-
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
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
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Q8RPZ8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Q9NSD9, Q9Y285
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
O95363
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Pseudomonas aeruginosa PAO01
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
O73984
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Q76KA8 and Q76KA8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Q5SGX2 and Q5SGX1
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
ir
additional information
?
-
-
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
Q8RPZ8
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
-
-
-
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
?
-
Q9NSD9
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
?
-
Q9Y285
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 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
-
-
-
additional information
?
-
Q76KA8 and Q76KA8
phylogenetic analysis
-
?
additional information
?
-
Q5SGX2 and Q5SGX1
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
ATP
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; optimal concentration is 20 mM
Zn2+
-
inhibition of tRNAPhe aminoacylation; 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+
-
maximal stimulation of 50fold to 100fold at 0.05 mM ZnCl2; 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(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
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
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-[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
-
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
(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
-
-
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-(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-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
-
-
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
-
-
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-[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-[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, Raynaud’s disease, and arthralgias, overview
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
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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
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.
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.
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.
Epilepsy
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
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.
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.
Myoclonus
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Neurodegenerative Diseases
A Newly Identified Missense Mutation in FARS2 Causes Autosomal-Recessive Spastic Paraplegia.
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.
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.
Seizures
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
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.
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
0.0018 - 0.05
L-Phe