6.1.1.20: phenylalanine-tRNA ligase
This is an abbreviated version!
For detailed information about phenylalanine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.20
-
6.1.1.20
-
aminoacylation
-
synthetases
-
aminoacyl-trna
-
phenylalanylation
-
thermophilus
-
thermus
-
anticodon
-
aarss
-
proofreading
-
phe-trnaphe
-
noncognate
-
tyrosyl-trna
-
misacylated
-
seryl-trna
-
threonyl-trna
-
misaminoacylated
-
mischarging
-
trna-phe
-
aminoacyladenylate
-
valyl-trna
-
alphabeta2
-
biotechnology
- 6.1.1.20
- aminoacylation
- synthetases
- aminoacyl-trna
-
phenylalanylation
- thermophilus
- thermus
-
anticodon
-
aarss
-
proofreading
- phe-trnaphe
-
noncognate
- tyrosyl-trna
-
misacylated
- seryl-trna
- threonyl-trna
-
misaminoacylated
-
mischarging
- trna-phe
-
aminoacyladenylate
- valyl-trna
-
alphabeta2
- biotechnology
Reaction
Synonyms
CML33, ctPheRS, cytoplasmic phenylalanyl-tRNA synthetase, cytosolic phenylalanyl-tRNA synthetase, cytosolic PheRS, EcPheRS, FARS2, FRS, hcPheRS, HSPC173, L-Phenylalanyl-tRNA synthetase, mitochondrial phenylalanyl-tRNA synthetase, mitochondrial PheRS, mitPheRS, More, mtPheRS, p-azido-phenylalanyl-tRNA synthetase, pAzFRS, Phe-RS, Phenylalanine translase, phenylalanine tRNA synthetase, 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, PheRS-alpha, Synthetase, phenylalanyl-transfer ribonucleate
ECTree
6.1.1.20 phenylalanine-tRNA ligaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 6.1.1.20 - phenylalanine-tRNA ligase
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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
-
-
-
-
?
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + 4-acetyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-acetyl-L-phenylalanyl-tRNAPhe
-
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
-
recombinant mutant A294G
-
?
ATP + 4-cyano-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-cyano-L-phenylalanyl-tRNAPhe
-
recombinant mutant A294G
-
?
ATP + 4-ethynyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-ethynyl-L-phenylalanyl-tRNAPhe
-
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
-
recombinant mutant A294G
-
?
ATP + benzofuranylalanine + tRNAPhe
AMP + diphosphate + L-benzofuranylalanyl-tRNAPhe
-
benzofuranylalanine is a substrate for aminoacylation of tRNAPhe by mutant enzyme with mutation A294G in the alpha-subunit
-
-
?
ATP + L-alanine + tRNAPhe
AMP + diphosphate + L-alanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
-
tRNAPhe variant, 370fold reduced activity compared to wild-type tRNAPhe
-
?
ATP + L-tryptophan + tRNAPhe
AMP + diphosphate + L-tryptophanyl-tRNAPhe
-
-
-
-
?
ATP + L-Tyr + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
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
-
-
?
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
-
-
?
GTP + L-phenylalanine + tRNAPhe
GMP + diphosphate + L-phenylalanyl-tRNAPhe
-
40fold lower activity compared to ATP
-
?
N6-methyladenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
N6-methyladenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
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
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + 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
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
-
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
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
-
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
overcharged product cannot be isolated from living cells
ir
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
0.13% activity compared to L-phenylalanine
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
0.33% activity compared to L-phenylalanine
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
recombinant mutant A294G
-
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
-
suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
-
-
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
-
suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
-
-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
1.9% activity compared to L-phenylalanine
-
-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
22% activity compared to L-phenylalanine
-
-
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
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
-
-
?
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
-
-
-
?
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
-
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
-
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
-
-
-
?
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
-
-
-
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 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 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
?
-
-
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
-
-
?
