Information on EC 6.1.1.20 - phenylalanine-tRNA ligase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
6.1.1.20
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
reaction mechanism in which ATP and phenylalanine enter the reaction in an obligatory ordered fashion. A random mechanism is not completely eliminated
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
reaction mechanism
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
mechanism, the reaction intermediate is bound to the active site cleft in the catalytic alpha-subunit
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
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
Q76KA8 and Q76KA8
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
substrate binding mechanism, residues S180, Q218, E220, W149, H178, R204, and Q218 are involved in binding of phenylalanine via hydrogen bonds
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
tRNA channeling mechanism
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
tRNA recognition and binding mode
Q9NSD9, Q9Y285
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
tRNAPhe substrate binding mechanism, base-specific interactions between the 3'-end of the tRNA and the enzymes alpha- and beta-subunit
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
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
O95363
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
residue N217 is essential for catalysis
O73984
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
-
-
-
-
esterification
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
phenylalanine metabolism
-
-
tRNA charging
-
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine:tRNAPhe ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CML33
-
-
-
-
FRS
-
-
-
-
HSPC173
-
-
-
-
L-Phenylalanyl-tRNA synthetase
-
-
-
-
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
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9055-66-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9Y9I6: alpha-subunit, Q9Y9I3: beta-subunit
Q9Y9I6 and Q9Y9I3
SwissProt
Manually annotated by BRENDA team
Aeropyrum pernix DSM 11879
Q9Y9I6: alpha-subunit, Q9Y9I3: beta-subunit
Q9Y9I6 and Q9Y9I3
SwissProt
Manually annotated by BRENDA team
mutant strain UA22 carrying both wild-type and mutant alleles of gene pheS due to polyploidy
UniProt
Manually annotated by BRENDA team
wild-type strain 168, overproduced in Escherichia coli JM109
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
2 activities
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-
Manually annotated by BRENDA team
overproducing strain carrying a hybrid pBR322 plasmid containing the pheS-pheT locus
-
-
Manually annotated by BRENDA team
p-fluorophenylalanine-resistant strain with Ala294Ser mutation
-
-
Manually annotated by BRENDA team
purified enzyme, strain CP78 and mutant relA- strain CP79
-
-
Manually annotated by BRENDA team
strain K
-
-
Manually annotated by BRENDA team
strain K-10
-
-
Manually annotated by BRENDA team
strain MRE-600
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-
Manually annotated by BRENDA team
strain NP37 carrying the thermosensitive point mutation A294G in the active site
-
-
Manually annotated by BRENDA team
Escherichia coli K
strain K
-
-
Manually annotated by BRENDA team
Escherichia coli K-10
strain K-10
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-
Manually annotated by BRENDA team
Escherichia coli MRE-600
strain MRE-600
-
-
Manually annotated by BRENDA team
Escherichia coli NP37
strain NP37 carrying the thermosensitive point mutation A294G in the active site
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-
Manually annotated by BRENDA team
strain Spain 7
-
-
Manually annotated by BRENDA team
Haemophilus influenzae Spain
strain Spain 7
-
-
Manually annotated by BRENDA team
alpha chain
SwissProt
Manually annotated by BRENDA team
beta chain
SwissProt
Manually annotated by BRENDA team
class II enzyme
SwissProt
Manually annotated by BRENDA team
mitochondrial isozyme, class II enzyme
UniProt
Manually annotated by BRENDA team
i.e. Lactobacillus amylovorus, several strains, e.g. strains 16698T and AD5, from Finnish porcine isolates, housekeeping gene pheS encoding the alpha-subunit
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-
Manually annotated by BRENDA team
Methanobacterium thermoautotrophicus
-
-
-
Manually annotated by BRENDA team
strain 489
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-
Manually annotated by BRENDA team
Moraxella catarrhalis 489
strain 489
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 133
-
-
Manually annotated by BRENDA team
strain WCUH29 and Oxford strain, genes pheS and pheT
-
-
Manually annotated by BRENDA team
Staphylococcus aureus 133
strain 133
-
-
Manually annotated by BRENDA team
Streptococcus pneumoniae G9A
strain G9A
-
-
Manually annotated by BRENDA team
KOD1, class II enzyme
Q76KA8 and Q76KA8
UniProt
Manually annotated by BRENDA team
-
Q5SGX2 and Q5SGX1
UniProt
Manually annotated by BRENDA team
class II enzyme
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
C9QTZ3
architecture of four helix-bundle interface, characteristic of class IIc heterotetrameric aaRSs, is changed, each of the two long helices belonging to CLM transformed into the coil-short helix structural fragments. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain
malfunction
-
mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
0.13% activity compared to L-phenylalanine, 0.33% activity compared to L-phenylalanine
-
-
?
ATP + 4-acetyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-acetyl-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant T251G, no activity with A294G
-
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant A294G
-
?
ATP + 4-bromo-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-bromo-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant A294G
-
?
ATP + 4-cyano-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-cyano-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant A294G
-
?
ATP + 4-ethynyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-ethynyl-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant A294G
-
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
show the reaction diagram
Escherichia coli, Escherichia coli NP37
-
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 + tRNAPhe
AMP + diphosphate + 4-iodo-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
recombinant mutant A294G
-
?
ATP + benzofuranylalanine + tRNAPhe
AMP + diphosphate + L-benzofuranylalanyl-tRNAPhe
show the reaction diagram
-
benzofuranylalanine is a substrate for aminoacylation of tRNAPhe by mutant enzyme with mutation A294G in the alpha-subunit
-
-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
show the reaction diagram
-
1.9% activity compared to L-phenylalanine, 22% activity compared to L-phenylalanine
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O73984
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q8RPZ8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q5SGX2 and Q5SGX1
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q76KA8 and Q76KA8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q9NSD9, Q9Y285
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q9NSD9, Q9Y285
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O95363
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O95363
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
discrimination between phenylalanine and 18 other naturally occuring amino acids, discrimination factors
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
tRNAs from E. coli and bean chloroplast are not aminoacylated
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
heterologous aminoacylation of tRNA with high selectivity for archaebacterial tRNA
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
aminoacylates native yeast tRNAPhe, activity with mutant yeast tRNAPhe transcripts
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
100% activity
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
activity is restricted to endogenous tRNA, highly specific for L-phenylalanine
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
reaction intermediate aminacyl-AMP stucture
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
the recognition of Phe through a mixture of van der Waals interactions and hydrogen bonds
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O95363
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
show the reaction diagram
-
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
show the reaction diagram
-
wild-type tRNAPhe substrate, enzyme interacts with the 3'-end of tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
cognate amino acid charging
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis, 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
show the reaction diagram
-
charging of cognate amino acid
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O73984
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
show the reaction diagram
-
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
show the reaction diagram
-
structure-activity relationship, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Q9Y9I6 and Q9Y9I3
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
show the reaction diagram
Staphylococcus aureus 133
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Streptococcus pneumoniae G9A, Haemophilus influenzae Spain
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli MRE-600
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli MRE-600
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Moraxella catarrhalis 489
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli K-10
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli K-10
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli NP37
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis, 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
show the reaction diagram
Escherichia coli NP37
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli K
-
-
-
-
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
show the reaction diagram
-
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-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
show the reaction diagram
-
tRNAPhe variant, 370fold reduced activity compared to wild-type tRNAPhe
-
?
ATP + L-Tyr + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
show the reaction diagram
-
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
show the reaction diagram
-
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-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
show the reaction diagram
-
0.089% activity compared to L-phenylalanine
-
-
?
N6-methyladenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
N6-methyladenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
-
GTP + L-phenylalanine + tRNAPhe
GMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
40fold lower activity compared to ATP
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
-
additional information
?
-
-
ATP-diphosphate exchange
-
-
-
additional information
?
-
-
ATP-diphosphate exchange
-
-
-
additional information
?
-
-
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
?
-
-
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
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
-
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
?
-
-
no activity with tRNAPhe-s4 U76, a tRNA variant harboring a 4-thiouridine residue in the 3'-end
-
?
additional information
?
-
O95363
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
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
?
-
Q5SGX2 and Q5SGX1
the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
-
?
additional information
?
-
Q8RPZ8
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
Q76KA8 and Q76KA8
phylogenetic analysis
-
?
additional information
?
-
Q9NSD9, 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
?
-
Q5SGX2 and Q5SGX1
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
-
?
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
?
-
-
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
?
-
-
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
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O73984
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q8RPZ8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q5SGX2 and Q5SGX1
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q76KA8 and Q76KA8
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Q9NSD9, Q9Y285
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
O95363
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
cognate amino acid charging
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Staphylococcus aureus 133, Streptococcus pneumoniae G9A, Haemophilus influenzae Spain, Moraxella catarrhalis 489
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli NP37
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
Escherichia coli NP37
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
show the reaction diagram
-
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
-
-
?
additional information
?
-
Q8RPZ8
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
Q76KA8 and Q76KA8
phylogenetic analysis
-
?
additional information
?
-
Q9NSD9, 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
?
-
Q5SGX2 and Q5SGX1
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
-
?
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 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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
not dependent on
ATP
Methanobacterium thermoautotrophicus
-
-
ATP
Q76KA8 and Q76KA8
-
ATP
O95363
mitochondrial isozyme, high concentration is required for maximal activity
ATP
-
a 15fold excess is required for optimal activity
GTP
-
40fold lower activity than with ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
can substitute for Zn2+ in diadenosine 5',5'''-P1,P4-tetraphosphate synthesis
Iron
Q8RPZ8
regulatory function in mutant strain UA22
KCl
-
optimal concentration is 10 mM
Mg2+
-
requires three Mg2+ in activation reaction (including the one in Mg2+)
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+
-
both MgP2O7- and Mg2P2O7 participate in the pyrophosphorolysis of the aminoacyl adenylate; optimal concentration is 20 mM
Mg2+
O95363
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+
-
required
spermine
O95363
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+
-
inhibition of tRNAPhe aminoacylation; required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
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+
-
influence of Zn2+ on partial reactions of diadenosine 5',5'''-P1,P4-tetraphosphate synthesis
Mn2+
-
not bound to the active site, located at the interface of alpha and beta subunits
additional information
-
enzyme metal binding site structure, overview
INHIBITORS
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
(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-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
(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
-
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-[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
-
-
1-(3-bromophenyl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 110 nM
1-(3-chlorophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 31 nM
1-(3-iodophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 32 nM
1-(3-methoxyphenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 83 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-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-[4-[(3-chlorobenzyl)oxy]-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
-
-
2',3'-Ribodeoxy-ATP
-
-
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-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
-
2-phenylacetamidine
-
competitive with respect to phenylalanine
2-[(2-methoxybenzyl)amino]-1-(3-methylphenyl)ethanol
-
IC50: 110 nM
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-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-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-(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-methyl-1,3,4-oxadiazole
-
-
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'-Deoxyadenosine 5'-triphosphate
-
-
3'-Methoxy-ATP
-
-
3'-Methyladenosine 5'-triphosphate
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
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-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
-
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-(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-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-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-hydroxycyclohexyl)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-[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
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-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-oxadiazole-2-carboxamide
-
-
Alkylamides of phenylalanine
-
the inhibitor constant decreases with increasing length of the alkyl chain
benzylguanidine
-
competitive with respect to phenylalanine
CTP
-
-
diphosphate
-
-
DL-m-tyrosine
-
;
DTT
-
-
E. coli tRNAPhe
-
inhibition by formation of a tight complex of the enzyme with the diphosphate formed during the aminoacylation
-
GTP
-
-
L-phenylalanyl-5'-adenylate
-
-
L-phenylalanyl-adenylate
-
-
L-tyrosine
-
-
L-tyrosyl-adenylate
-
-
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
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-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
-
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
-
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-benzyl-D-amphetamine
-
most potent competitive inhibitor, selectivity for bacterial enzyme
N-benzylbenzamidine
-
competitive with respect to phenylalanine
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
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
-
IC50: 120 nM
N6-Benzyladenosine 5'-triphosphate
-
-
ochratoxin A
-
-
Ochratoxine
-
-
Ochrotoxine A
-
cometitive
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-sulfonamido-aminoethyl-chloroindol
-
-
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindole
-
-
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindole
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
PheOH-AMP
-
-
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
tRNAPhe Cp75
-
tRNAPhe with cytosine phosphate residue at position 75
-
tRNAPhe s4-U75
-
tRNAPhe with 4-thiouridine residue at position 75
-
tRNAPhe s4-U76
-
tRNAPhe with 4-thiouridine residue at position 76
-
tRNAPhe s4-U77
-
tRNAPhe with 4-thiouridine residue at position 77
-
tRNAPhe s4-Up77
-
tRNAPhe with 4-thiouridine phosphate residue at position 77
-
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
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
-
IC50: 49 nM
[3-chloro-4-[(3-chlorobenzyl)oxy]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-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
-
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
additional information
Q8RPZ8
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynauds disease, and arthralgias, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
activates
elongation factor 1alpha
-
interaction enhances the activity
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
additional information
Q8RPZ8
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00016
(s-pA)tRNAPhe
-
-
-
0.00017
(s-pG)tRNAPhe
-
-
-
0.085
2'-Deoxyadenosine 5'-triphosphate
-
mitochondrial
0.125
2'-Deoxyadenosine 5'-triphosphate
-
-
0.19
2'-Deoxyadenosine 5'-triphosphate
-
cytoplasmic
0.4
2'-Deoxyadenosine 5'-triphosphate
-
cytoplasmic
0.05
2-Chloroadenosine 5'-triphosphate
-
aminoacylation
0.096
2-Chloroadenosine 5'-triphosphate
-
mitochondrial
0.11
2-Chloroadenosine 5'-triphosphate
-
-
0.16
2-Chloroadenosine 5'-triphosphate
-
cytoplasmic
0.16
2-Chloroadenosine 5'-triphosphate
-
mitochondrial
0.2
2-Chloroadenosine 5'-triphosphate
-
-
0.2
2-Chloroadenosine 5'-triphosphate
-
cytoplasmic, 2'-deoxyadenosine 5'-triphosphate; mitochondrial, 3'-deoxyadenosine 5'-triphosphate
1.54
2-deoxyadenosine 5'-triphosphate
-
aminoacylation
0.3
3'-deoxadenosine 5'-triphosphate
-
cytoplasmic
0.82
3'-Deoxyadenosine 5'-triphosphate
-
aminoacylation
1
3'-Deoxyadenosine 5'-triphosphate
-
mitochondrial
0.38
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.6
3,4-dihydroxy-L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.65
3,4-dihydroxy-L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.0058
ATP
-
-
0.008
ATP
-
cytoplasmic
0.009
ATP
-
-
0.03
ATP
-
-
0.055
ATP
-
mitochondrial
0.055
ATP
-
ATP, , mitochondrial, aminoacylation
0.06
ATP
-
aminoacylation
0.065
ATP
-
mitochondrial
0.065
ATP
-
aminoacylation; mitochondrial
0.08
ATP
-
cytoplasmic, aminoacylation
0.08
ATP
-
ATP
0.1
ATP
-
25C
0.122
ATP
-
recombinant enzyme, pH 7.9, 22C
0.14
ATP
-
cytoplasmic
0.14
ATP
-
ATP, , cytoplasmic, aminoacylation
0.147
ATP
-
native enzyme, pH 7.9, 22C
0.62
ATP
-
mitochondrial, ATP-diphosphate exchange
0.7
ATP
-
mitochondrial, ATP-diphosphate exchange
0.84
ATP
-
cytoplasmic, ATP-diphosphate exchange
0.9
ATP
-
cytoplasmic, ATP-diphosphate exchange
2.5
ATP
O95363
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37C
923
benzofuranylalanine
-
-
0.012
DL-m-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.13
DL-m-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.0018
L-Phe
-
-
0.0042
L-Phe
-
pH 7.2, 37C, mitochondrial enzyme
0.0103
L-Phe
-
wild-type enzyme
0.0212
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit
0.0225
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
0.0261
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
0.0282
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
0.03
L-Phe
-
pH 7.2, 37C, cytosolic enzyme
0.0312
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
0.0331
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
0.00048
L-phenylalanine
-
pH 7.8, 60C
0.00094
L-phenylalanine
-
recombinant enzyme, pH 7.9, 22C
0.0012
L-phenylalanine
-
native enzyme, pH 7.9, 22C
0.0015
L-phenylalanine
-
25C
0.0015
L-phenylalanine
-
pH 7.8, 70C
0.0017
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.002
L-phenylalanine
-
wild-type EcPheRS
0.0026
L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.003
L-phenylalanine
-
wild-type ctPheRS
0.0032
L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.0045
L-phenylalanine
-
mutant A294G EcPheRS
0.0049
L-phenylalanine
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G
0.005
L-phenylalanine
-
wild-type mtPheRS
0.0053
L-phenylalanine
-
pH 7.2, 37C, full-length PheRSA294G
0.017
L-phenylalanine
-
mutant A333G mtPheRS
0.033
L-phenylalanine
O95363
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37C
0.233
L-phenylalanine
-
mutant G458A ctPheRS
0.86
L-Tyr
-
pH 7.2, 37C, cytosolic enzyme
0.32
L-tyrosine
-
mutant A294G EcPheRS
0.637
L-tyrosine
-
wild-type ctPheRS
0.66
L-tyrosine
-
mutant A333G mtPheRS
1.155
L-tyrosine
-
wild-type mtPheRS
1.9
L-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
2.2
L-tyrosine
-
wild-type EcPheRS
0.81
N6-methyladenosine 5'-triphosphate
-
aminoacylation
0.00045
Phe
-
-
0.007
Phe
-
-
0.0094
Phe
-
cytoplasmic, aminoacylation
0.011
Phe
-
mitochondrial, aminoacylation
0.012
Phe
-
mitochondrial, aminoacylation
0.013
Phe
-
cytoplasmic, aminoacylation
0.028
Phe
-
-
0.029
Phe
-
mitochondrial, ATP-diphosphate exchange
0.033
Phe
-
cytoplasmic, ATP-diphosphate exchange
0.034
Phe
-
mitochondrial, ATP-diphosphate exchange
0.038
Phe
-
mitochondrial, ATP-diphosphate exchange
0.083
Phe
-
-
0.000066
tRNAPhe
-
-
0.0001
tRNAPhe
-
recombinant heterodimer, pH 8.0, 25C
0.00011
tRNAPhe
-
recombinant His-tagged heterodimer, pH 8.0, 25C
0.00012
tRNAPhe
-
substrate from yeast, , aminoacylation
0.00016
tRNAPhe
-
-
0.00017
tRNAPhe
-
substrate from yeast
0.0002
tRNAPhe
-
substrate from calf liver, , cytoplasmic, aminoacylation
0.00042
tRNAPhe
-
cytoplasmic enzyme, aminoacylation
0.00042
tRNAPhe
-
mitochondrial enzyme, calf liver tRNAPhe
0.00052
tRNAPhe
-
substrate from calf liver, , mitochondrial, aminoacylation
0.00058
tRNAPhe
-
substrate from calf liver, , mitochondrial, aminoacylation
0.00065
tRNAPhe
-
substrate from yeast, , aminoacylation
0.00078
tRNAPhe
-
substrate from yeast, , mitochondrial, aminoacylation
0.0022
tRNAPhe
-
pH 7.2, 37C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.0025
tRNAPhe
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.0027
tRNAPhe
-
pH 7.2, 37C, full-length PheRSA294G, substrate from Escherichia coli
0.0032
tRNAPhe
-
substrate from E. coli
0.0041
tRNAPhe
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.018
tRNAPhe
O95363
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37C
3
L-tyrosine
-
mutant G458A ctPheRS
additional information
additional information
-
negative cooperativity exists in the binding of all substrates
-
additional information
additional information
-
Km-value for tRNA mutants
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
Km value for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics, binding energies in the active conformation
-
additional information
additional information
-
full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview
-
additional information
additional information
-
aminoacylation kinetics with Phe and Tyr
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
3,4-dihydroxy-L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.16
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.23
3,4-dihydroxy-L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
2.9
ATP
O95363
ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37C
2.3
benzofuranylalanine
-
-
0.052
DL-m-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.65
DL-m-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.975
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
1.72
L-Phe
-
wild-type enzyme
2.04
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit
2.645
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
2.88
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
3 - 6
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
3.12
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
3.3
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
6.08
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
150
L-Phe
-
pH 7.2, 37C, mitochondrial enzyme
240
L-Phe
-
pH 7.2, 37C, cytosolic enzyme
0.055
L-phenylalanine
-
pH 7.8, 60C
0.075
L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.115
L-phenylalanine
-
pH 7.8, 70C
0.87
L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
1.1
L-phenylalanine
O95363
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37C
1.12
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
3.27
L-phenylalanine
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G
3.34
L-phenylalanine
-
pH 7.2, 37C, full-length PheRSA294G
140
L-phenylalanine
-
mutant A333G mtPheRS
180
L-phenylalanine
-
wild-type mtPheRS
185
L-phenylalanine
-
mutant A294G EcPheRS
199
L-phenylalanine
-
wild-type EcPheRS
464
L-phenylalanine
-
mutant G45A8 ctPheRS
603
L-phenylalanine
-
wild-type ctPheRS
160
L-Tyr
-
pH 7.2, 37C, cytosolic enzyme
0.033
L-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.6
L-tyrosine
-
mutant G458S ctPheRS
5
L-tyrosine
-
wild-type mtPheRS
12.5
L-tyrosine
-
mutant A333G mtPheRS
35
L-tyrosine
-
wild-type EcPheRS
184
L-tyrosine
-
wild-type ctPheRS
0.077
tRNAPhe
-
pH 7.2, 37C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.11
tRNAPhe
O95363
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37C
0.11
tRNAPhe
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.78
tRNAPhe
-
pH 7.2, 37C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.82
tRNAPhe
-
pH 7.2, 37C, full-length PheRSA294G, substrate from Escherichia coli
185
L-tyrosine
-
mutant A294G EcPheRS
additional information
additional information
-
turnover numbers for tRNA mutants
-
additional information
additional information
-
turnover numbers for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
turnover numbers for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
turnover numbers for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
turnover-number of tRNAPheG34A is 10% of wild-type value, turnover-number of tRNAPheG34C/A35U is 31% of wild-type value, turnover-number of tRNAPheA36C is 4.2% of wild-type value, turnover-number of tRNAPheU20A is identical to wild-type value, turnover-number of tRNAPheG44C is 2.1% of wild-type value, turnover-number of tRNAPheG19U/C56G is 1.7% of wild-type value
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
3,4-dihydroxy-L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
2636
0.37
3,4-dihydroxy-L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
2636
0.43
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
2636
4.3
DL-m-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
177549
5
DL-m-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
177549
28.3
L-phenylalanine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
104
270
L-phenylalanine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
104
650
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
104
0.017
L-tyrosine
-
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
109
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000067
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.0037
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.00028
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.011
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.000011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00015
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.00036
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.046
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
larger than 0.064
0.0000017
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000126
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.0000031
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.000087
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
larger than 0.064
0.23
2-phenylacetamidine
-
-
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.000156
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.0000055
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.000081
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.0000015
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.000036
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.0000021
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000053
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.000076
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.0000066
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000095
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000029
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000483
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000022
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000254
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000057
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.000393
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.0000019
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000079
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000014
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.000438
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
larger than 0.064
0.0024
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.023
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
larger than 0.064
0.000012
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000097
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000024
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000043
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000046
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000016
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.0000015
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.000028
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.00003
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.00005
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.000008
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000065
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000038
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0013
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0000023
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.000042
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.0000026
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.000081
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.00005
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
0.0000027
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.00006
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.077
benzylguanidine
-
-
0.0136
DL-m-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.15
DL-m-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.085
L-phenylalanyl-5'-adenylate
-
versus ATP
0.089
L-phenylalanyl-5'-adenylate
-
versus L-Phe
3.1
L-Tyr
-
versus L-Phe
3.4
L-tyrosine
-
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30C
0.043
L-tyrosyl-adenylate
-
versus ATP
0.045
L-tyrosyl-adenylate
-
versus L-Phe
0.0000087
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
0.00012
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
0.000017
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.000091
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.00003
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
0.00016
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.0065
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
0.064
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
larger than 0.064
0.00017
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
0.0035
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
0.0035
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
0.0061
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
0.000034
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
0.000097
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
0.0031
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.012
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
larger than 0.064
0.00013
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
0.002
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
larger than 0.064
0.057
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
-
0.00024
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0022
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0000013
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000028
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.00014
N-benzyl-D-amphetamine
-
-
0.058
N-benzylbenzamidine
-
-
0.000021
phenyl-thiazolylurea-sulfonamido-aminoethylindole
-
pH 7.6, 22C
0.0002
PheOH-AMP
-
25C
0.00069
tRNAPhe Cp75
-
25C
-
0.00071
tRNAPhe s4-U75
-
25C
-
0.00064
tRNAPhe s4-U76
-
25C
-
0.0004
tRNAPhe s4-U77
-
25C
-
0.00035
tRNAPhe s4-Up77
-
25C
-
0.00015
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0023
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.00084
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0000019
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.000012
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.0064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
0.064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
0.064
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
larger than 0.064
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.0026 mM
0.0031
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.0031 mM
0.00047
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00047 mM
0.00051
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00051 mM
0.00017
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00017 mM
0.00026
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00026 mM
0.00017
(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
0.0016
(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
0.002
(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
0.00001
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 10 nM
0.00007
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 70 nM
0.0006
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 600 nM
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 40 nM, high selectivity over the human enzyme
0.00073
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00073 mM, high selectivity over the human enzyme
0.00099
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00099 mM, high selectivity over the human enzyme
0.003
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.003 mM, high selectivity over the human enzyme
0.004
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.004 mM, high selectivity over the human enzyme
0.0061
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0061 mM, high selectivity over the human enzyme
0.0087
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0087 mM, high selectivity over the human enzyme
0.00056
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00056 mM, high selectivity over the human enzyme
0.00085
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00085 mM, high selectivity over the human enzyme
0.00007
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00007 mM, high selectivity over the human enzyme
0.00022
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00022 mM, high selectivity over the human enzyme
0.000002
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 2 nM, high selectivity over the human enzyme
0.000005
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM, high selectivity over the human enzyme
0.0083
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0083 mM, high selectivity over the human enzyme
0.0137
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0137 mM, high selectivity over the human enzyme
0.032
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.032 mM, high selectivity over the human enzyme
0.045
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.045 mM, high selectivity over the human enzyme
0.000004
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 4 nM
0.000005
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM
0.00013
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 130 nM
0.011
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
-
IC50: 0.011 mM
0.033
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
-
IC50: 0.033 mM
0.00082
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 820 nM
0.0032
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 3200 nM
0.00011
1-(3-bromophenyl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 110 nM
0.000031
1-(3-chlorophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 31 nM
0.000032
1-(3-iodophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 32 nM
0.000083
1-(3-methoxyphenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 83 nM
0.000015
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 15 nM
0.00005
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 50 nM
0.00005
1-(4-bromothiophen-2-yl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 50 nM
0.00012
1-(4-bromothiophen-2-yl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 120 nM
0.000026
1-(4-bromothiophen-2-yl)-2-[(2-[[4-(methylsulfonyl)benzyl]oxy]benzyl)amino]ethanol
-
IC50: 26 nM
0.000008
1-(4-bromothiophen-2-yl)-2-[[2-(2-hydroxyethoxy)benzyl]amino]ethanol
-
IC50: 8 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(but-3-en-1-yloxy)benzyl]amino]ethanol
-
IC50: 18 nM
0.000035
1-(4-bromothiophen-2-yl)-2-[[2-(methoxymethoxy)benzyl]amino]ethanol
-
IC50: 35 nM
0.000043
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-2-ylmethoxy)benzyl]amino]ethanol
-
IC50: 43 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-3-ylmethoxy)benzyl]amino]ethanol
-
IC50: 18 nM
0.000016
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-4-ylmethoxy)benzyl]amino]ethanol
-
IC50: 16 nM
0.00057
1-[3-(hydroxymethyl)phenyl]-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 570 nM
0.00011
2-[(2-methoxybenzyl)amino]-1-(3-methylphenyl)ethanol
-
IC50: 110 nM
0.00019
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethoxy)phenyl]ethanol
-
IC50: 190 nM
0.00016
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 160 nM
0.00079
2-[(2-methylbenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 790 nM
0.0025
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]benzoic acid
-
IC50: 2500 nM
0.0001
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]phenol
-
IC50: 100 nM
0.00011
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)acetamide
-
IC50: 110 nM
0.000032
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-ethylacetamide
-
IC50: 32 nM
0.000042
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetamide
-
IC50: 42 nM
0.000022
2-[4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butyl]-1H-isoindole-1,3(2H)-dione
-
IC50: 22 nM
0.000026
2-[[2-(1H-benzimidazol-2-ylmethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 26 nM
0.00022
2-[[2-(2-aminoethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 220 nM
0.000022
2-[[2-(4-aminobutoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 22 nM
0.00001
2-[[2-(benzyloxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 10 nM
0.00005
2-[[2-(benzyloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 50 nM
0.00026
2-[[2-(difluoromethoxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 260 nM
0.000058
2-[[2-(prop-2-en-1-yloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 58 nM
0.000025
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)propanamide
-
IC50: 25 nM
0.000036
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]propanamide
-
IC50: 36 nM
0.000058
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]propanoic acid
-
IC50: 58 nM
0.000026
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)butanamide
-
IC50: 26 nM
0.00003
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]butanamide
-
IC50: 30 nM
0.000043
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butanoic acid
-
IC50: 43 nM
0.000008
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 8 nM
0.00005
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 50 nM
0.00012
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
-
IC50: 120 nM
0.000049
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
-
IC50: 49 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.074
-
purified native enzyme
0.12
-
purified recombinant enzyme
0.124
-
-
0.19
-
pure enzyme
0.21
-
purified enzyme, 37C
0.31
-
purified recombinant enzyme expressed in Escherichia coli, 37C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
2-(morpholino)ethanesulfonic acid buffer or 2-(2-hydroxy-1,1-bis(hydroxymethyl)ethyl)aminoethanesulfonic acid buffer
7
Q76KA8 and Q76KA8
assay at
7.2
-
assay at
7.2
-
assay at, aminoaclyation
7.3
O95363
ATP-diphosphate exchnage assay at
7.5 - 8.1
-
assay at
7.5
Q9NSD9, Q9Y285
assay at
7.5
O95363
aminoacylation assay at
7.5
-
assay at
7.5
-
assay at
7.9
-
assay at
8
-
broad maximum
8
-
assay at
8
Q9NSD9, Q9Y285
tRNA aminoacylation assay; tRNA aminoacylation assay
8.5
-
Tris/HCl buffer
8.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
no activity below pH 6.0 and above 8.5, higher activity range is pH 6.5-8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
25
-
assay at
25
-
aminoacylation assay
25
Q9NSD9, Q9Y285
tRNA aminoacylation assay; tRNA aminoacylation assay
30
-
assay at
37
Q9NSD9, Q9Y285
assay at
37
O95363
assay at
37
-
assay at
37
-
assay at, aminoaclyation
43
-
ATP-diphosphate exchange
70
-
E. coli tRNAPhe, aminoacylation
80
-
Thermus thermophilus tRNAPhe, aminoacylation
85
-
ATP-diphosphate exchange
95
Q76KA8 and Q76KA8
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
no activity at 10C and 50C
55 - 90
-
55C: about 50% of maximal activity, 90C: about 65% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
Q76KA8 and Q76KA8
beta-subunit
6.4
-
sequence calculation
9.4
Q76KA8 and Q76KA8
alpha-subunit
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q9NSD9, Q9Y285
lung carcinoma cell line
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
high content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
promyelocytic leukemia cell line, high content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
chronic myelogenous leukemic cell line, high content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
low content, embryonic and adult
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
low content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
low content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
low content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
-
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
colorectal adenocarcinoma cell line, high content
Manually annotated by BRENDA team
Q9NSD9, Q9Y285
lymphoblastic leukemia cell line
Manually annotated by BRENDA team
additional information
Q9NSD9, Q9Y285
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacteroides fragilis (strain ATCC 25285 / NCTC 9343)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Staphylococcus haemolyticus (strain JCSC1435)
Staphylococcus haemolyticus (strain JCSC1435)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38200
Q9NSD9, Q9Y285
alpha-subunit, mutant DELTA1-175, determined by SDS-PAGE
706791
40000
-
alpha-subunit of recombinant enzyme, mass spectroscopy
653736
45000
O95363
recombinant mitochondrial isozyme, gel filtration
652794
45000
-
mitPheRS, gel filtration
695155
45000
Q9NSD9, Q9Y285
alpha-subunit, mutant DELTA60-170, determined by SDS-PAGE
706791
48000
O95363
recombinant mitochondrial isozyme, analytical velocity sedimentation centrifugation
652794
48000
-
recombinant enzyme, gel filtration
671135
48000
-
monomer, determined by SDS-PAGE
703722
49600
O95363
recombinant mitochondrial isozyme, amino acid sequence determination
652794
57500
Q9NSD9, Q9Y285
alpha-subunit, wild-type, determined by SDS-PAGE
706791
67000
Q9NSD9, Q9Y285
beta-subunit, wild-type, determined by SDS-PAGE
706791
71000
-
binary mitPheRS-tRNAPhe complex, gel filtration
695155
78000
-
gel filtration
352
89090
-
beta-subunit of recombinant enzyme, mass spectroscopy
653736
96000
-
dimer, mutant, crosslinked subunits
703722
183000
-
gel filtration
330
240000
-
gel filtration
650377
245000
-
gel filtration
313
247000
-
heterotetramer
701539
250000
-
gel filtration
345
255000
-
gel filtration
338
260000
-
-
312
260000
-
gel filtration
346
260000
-
gel filtration
349
260000
-
gel filtration
352
260000
-
-
352
260000
-
gel filtration
352
260000
Methanobacterium thermoautotrophicus
-
gel filtration
650424
266000
-
gel filtration
334
267000
-
high speed analytical ultracentrifugation, gel filtration
330
270000
-
gel filtration
309
270000
-
gel filtration
347
270000
-
gel filtration
722296
297000
-
recombinant enzyme, dynamic light scattering at 20
653743
350000
-
gel filtration
332
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
?
-
x * 59000 (alpha) + x * 72000 (beta)
?
-
x * 80000, SDS-PAGE
?
Q76KA8 and Q76KA8
x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
?
-
x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
dimer
-
-
dimer
-
1 * 33000 (alpha) + 1 * 42000 (beta), SDS-PAGE
dimer
Q9NSD9, Q9Y285
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
dimer
Q9NSD9, Q9Y285
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
heterodimer
-
1 * 54000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE
heterotetramer
-
build of two alphabeta heterodimers
heterotetramer
-
ctPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
heterotetramer
-
EcPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
heterotetramer
-
two alpha and two beta subunits
heterotetramer
C9QTZ3
EcPheRS is a (alphabeta)2 heterotetramer, built of two alphabeta heterodimers
monomer
-
-
monomer
O95363
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
monomer
-
1 * 48000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 49600, sequence calculation
oligomer
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
oligomer
Escherichia coli NP37
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
-
tetramer
-
-
tetramer
-
2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
tetramer
-
2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE
tetramer
-
2 * 57000 (alpha) + 2 * 66000 (beta), SDS-PAGE
tetramer
-
2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
tetramer
-
2 * 63000 (alpha) + 2 * 70000 (beta), SDS-PAGE
tetramer
-
2 * 98000 (alpha) + 2 * 38000 (beta), SDS-PAGE
tetramer
-
2 * 57000 (alpha) + 2 * 72000 (beta), urea-SDS PAGE
tetramer
-
2 * 40000, alpha subunit, + 2 * 90000, beta-subunit, (alphabeta)2, recombinant enzyme, SDS-PAGE
tetramer
-
2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
Methanobacterium thermoautotrophicus
-
2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
tetramer
-
(alphabeta)2 heterotetramer
tetramer
-
PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview
tetramer
Q9Y9I6 and Q9Y9I3
2 * alpha + 2 * beta
tetramer
Aeropyrum pernix DSM 11879
-
2 * alpha + 2 * beta
-
tetramer
Escherichia coli K-10
-
2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
-
monomer
-
mtPheRS, alpha-subunit monomer, catalytic domain
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
all forms of homologous subunits have no catalytic activity
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
-
the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
additional information
-
the amino terminal part of each beta-subunit represents the main tRNA binding domain and is not involved in either catalysis or subunit interactions. The trypsin resistant alpha2beta2 core contains the catalytic site as well as contact areas between subunits
additional information
-
enzyme is part of an aminoacyl-tRNA synthetase complex which is resistant to dissociation when subjected to gel filtration
additional information
-
both alpha- and beta-subunits mainly exist in the dimeric form
additional information
-
alphabeta organization, the alpha-subunit is the catalytically active one
additional information
Q9NSD9, 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
Q5SGX2 and Q5SGX1
the enzyme is modularly composed of several different domains
additional information
O95363
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
-
human mitPheRS is a chimera of the bacterial beta-subunit of PheRS and the B8 domain of its beta-subunit, together, the beta-subunit and the RNP-domain, i.e. B8 domain, at the C-terminus form the minimal structural set to construct an enzyme with phenylalanylation activity, overview
additional information
O73984
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
-
human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview
additional information
-
structure analysis and structure-activity relationship, overview
additional information
C9QTZ3
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
-
structure molecular dynamics simulations of hmtPheRS, wild-type and mutant enzymes, overview
additional information
Escherichia coli MRE-600
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity, beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers, the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the large subunit of the mitochondrial enzyme is a glycoprotein with nearly 3% carbohydrate by weight. The carbohydrates present are: glucose, N-acetylglucosamine, mannose, galactose and N-acetylneuraminic acid
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and SeMet-labeled PheRs in complex with phenylalanine and AMP, hanging-drop vapor-diffusion method, 20C using 0.004 ml of protein solution, containing 10 mg/ml protein and 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 1 mM EDTA, 1 mM MgCl2, 10% glycerol, 1 mM Phe and 1 mM ATP, are mixed at 1:1 ratio with precipitant containing 17-20% PEG 8000K, 0.2 M MgCl2, 0.1 M Tris-HCl buffer, pH 8.5, 3% 1,6 hexandiol, and 3% D-galactose, 3 days, mother-liquor solution containing 20% v/v ethylene-glycol, X-ray diffraction structure determination and analysis at 3.05 A resolution
C9QTZ3
in complex with 3,4-dihydroxy-L-phenylalanine; in complex with 3,4-dihydroxy-L-phenylalanine
-
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
purified recombinant mitPheRS in complex with L-phenylalanine and ATP, hanging or sitting drop vapour diffusion method, 0.001-0.003 ml of protein solution containing 6 mg/ml protein in 20 mM Tris-HCl pH 8.0, 100 mM NaCl, 7 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM EDTA and 0.0065% NaN3, is mixed with an equal volume of reservoir solution containing 25 mM Tris-HCl pH 8.5, 10 mM MgCl2, 5 mM ATP, 2 mM L-phenylalanine, equilibration against reservoir solution, at 4C or 19C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
the structure of cytosolic phenylalanyl-tRNA synthetase in complex with phenylalanine is solved to 3.3 A resolution; the structure of cytosolic phenylalanyl-tRNA synthetase in complex with phenylalanine is solved to 3.3 A resolution
Q9NSD9, Q9Y285
the structure of human cytoplasmic phenylalanyl-tRNA synthetase is determined to a resolution of 3.3 A
-
purified recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit, 0.001 ml of protein solution containing 36 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl, mixed with 0.001 ml of precipitant solution, containing 100 mM sodium citrate, pH 5.6, and 16.5% PEG 20000, covarage with a 1:1 mixture of paraffin oil and silicone, 20C, 1 week, soaking in a soaked in a cryoprotectant solution containing 100 mM sodium citrate, pH 5.6, 18.2% PEG 20000, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
O73984
native enzyme crystals are of poor quality diffracting only to 3-5 A resolution, engineered mutant enzymes diffracts to 2.0 A resolution, X-ray diffraction structure determination and analysis, overview
-
at 0.6-nm resolution
-
crystal structure at 2.9 A resolution
-
crystal structure of complexes of enzyme with L-Tyr, p-chlorophenylalanine, and L-tyrosyl-adenylate
-
crystal structure of enzyme complexed with cognate tRNAPhe
-
enzyme complexed with phenylalanine or the phenylalanyl-adenylate analogue phenylalaninyl-adenylate, X-ray diffraction structure determination at 2.7 and 2.5 A resolution, respectively, and analysis
-
in complex with 3,4-dihydroxy-L-phenylalanine
-
native enzyme complexed with phenylalanyl-adenylate in presence of manganese, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
PheRS in complex with with cognate tRNAPhe and nonhydrolyzable phenylalanyladenylate analogue PheOH-AMP, hanging-drop vapor-diffusion method, 4C, 3-5 mg/ml protein ina ratio of 1:2,5 with tRNAPhe in 20 mM imidazole-HCl, pH 7.8, 1 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM NaN3, 10% saturated ammonium sulfate, and 1 mM PheOH-AMP, slow equilibration against a reservoir solution containing the crystallization buffer and 27% saturated ammonium sulfate, cryoprotection by 30% v/v glycerol, X-ray diffraction structure determination and anaylsis at 3.1 A resolution, modeling
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5 - 8
-
high stability of wild-type and mutant mtPheRSs in the pH range, unfolding parameters, overview
715937
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44
-
about 50% loss of activity after 50 min
323
55
-
15 min, 50% loss of activity
335
70
-
4 h, stable
722296
88
-
10 min, 50% inactivation
650377
90
-
about 30% loss of activity after 80 min
323
90
-
1 h, 50% loss of activity
722296
95
-
about 45% loss of activity after 20 min
323
98
Q76KA8 and Q76KA8
enzyme retains its tertiary structure
651809
100
-
the enzyme is almost completely destroyed within 3 min
722296
additional information
-
preincubation with ATP stabilizes against thermal inactivation
335
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol
-
-70C, purified recombinant His-tagged mitochondrial isozyme, 50 mM Tris-HCl, pH 7.6, 50 mM KCl, 10 mM MgCl2, 7 mM 2-mercaptoethanol, 10% v/v glycerol, small aliquots, stable for at least 6 months
O95363
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged proteins from Escherichia coli strain M15 by nickel affinity chromatography, complex formation of the two subunits during purification
-
recombinant His-tagged PheRs from Escherichia coli
C9QTZ3
;
Q9NSD9, Q9Y285
a TALON metal affinity resin column is applied
-
ammonium sulfate fractionation is followed by four chromatography columns, anion exchange on a DEAE-Sepharose column, a heparin-Sepharose column, concentrating the protein on a TSK hydrophobic interaction column and finally gel filtration on a column of superfine Sephadex G-200
-
glutathione Sepharose column chromatography
-
His6-tagged proteins are purified on nickel-nitrilotriacetic acid-agarose
-
mature mitPheRS in Escherichia coli by streptomycin precipitation, ultrafiltration, anion exchange chromatography and heparin affinity chromatography, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
recombinant His-tagged heterodimers and nontagged subunits from Escherichia coli, over 200fold
-
to homogeneity
Methanobacterium thermoautotrophicus
-
recombinant N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain B834(DE3) by anion exchange chromatography, adsorption chromatography, and gel filtration
O73984
His6-tagged proteins are purified on nickel-nitrilotriacetic acid-agarose
-
native enzyme from Oxford strain, 50% purity, recombinant enzyme overexpressed in Escherichia coli, over 90% purity
-
recombinant alpha- and beta-subunit both expressed in Escherichia coli
Q76KA8 and Q76KA8
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q9Y9I6 and Q9Y9I3
expression of genes pheS and pheT with an iron-repressible luxAB-reporter activity, which is promotorless due to mutagenic modification, expression is repressed under iron-sufficient conditions and derepressed under iron-limited conditions
Q8RPZ8
overproduced in Escherichia coli
-
two genes encoding subunits alpha and beta, DNA and amino acid sequence determination and analysis, expression as His-tagged proteins in Escherichia coli strain M15
-
expression of wild-type and mutant pheS, alpha-subunit encoding, gene in different Burkholderia species, e.g. Burkholderia thailandensis, allelic replacement
-
complementatiom of a growth mutant defective in phenylalanylation in vivo by wild-type full-length PheRS from Saccharomyces cerevisiae, the full-length Escherichia coli enzyme A294G, and the truncated mutant PheRSDELTAB2, overexpression of full-length mutant A294G and truncated mutant PheRSDELTAB2A294G in strain XL-1 Blue
-
expression of His-tagged PheRs in Escherichia coli
C9QTZ3
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Eed-IYRS, overview
-
mutant genes
-
overexpression of mutants
-
;
Q9NSD9, Q9Y285
DNA and amino acid sequence determination of the alpha- and beta-subunit and analysis, expression in COS-7 cells
Q9NSD9, Q9Y285
DNA and amino acid sequence determination, individual cloning and coexpression of His-tagged alpha- and beta-subunits in Escherichia coli resulting in 3 different types of (alphabeta)2 heterodimers with the His-tag at the N-terminus, N-terminally His-tagged beta-subunit renders the enzyme inactive, overexpression of nontagged alpha- and beta-subunits in Escherichia coli
-
Escherichia coli pET21c+ encoding human mtPheRS, FARS2, produces mature His6-tagged wild-type PheRS
-
Escherichia coli strain BL21(pArgU218)/pET21c-PheRS expresses C-terminal His6-tagged mtPheRS, RosettaDE3 cells containing pRARE plasmids encoding tRNAs for rare codons are transformed with the mutant mtPheRS plasmid constructs
-
expressed in Escherichia coli Tuner cells
-
mature mitPheRS in Escherichia coli without His-tag, which causes oligomerization of the recombinant enzyme during purification
-
mitochondrial isozyme, DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme
O95363
the two subunits of hcPheRS are cloned into two different plasmids, the alpha subunit, residues 1-508, into the vector pET21b+, the beta-subunit, residues 1-589, into pET28b+, for expression in Escherichia coli BLRDE3 cells, no affinity tag is used
-
pheS, DNA and amino acid sequence determination and analysis, phylogenetic analysis by multilocus sequence analysis, overview
-
DNA sequence determination and analysis
Methanobacterium thermoautotrophicus
-
expression of N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain B834(DE3)
O73984
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ped-IYRS, overview
-
Escherichia coli BL21-RIL/pET16b produces His6-tagged mtPheRS encoded by the MSF1 gene, the ctPheRS alpha and beta subunits, encoded by the FRS1 and FRS2 genes, respectively, are expressed in tandem from pQE31-FRS-sc in Escherichia coli BL21-RIL cells
-
genes pheS and pheT encoding the alpha and beta subunits in one transcriptional operon, DNA and amino acid sequence determination and analysis, overexpression of both genes in an artificial operon in Escherichia coli
-
expression of wild-type and mutant enzymes
-
genes encoding alpha- and beta-subunit, DNA and amino acid sequence determination and analysis, expression of alpha-subunit and of beta-subunit in Escherichia coli
Q76KA8 and Q76KA8
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ted-IYRS, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A249G/A356W
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit, kcat/Km is 6.6% of wild-type value
A249G/E334A
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit, kcat/Km is 60% of wild-type value
A249G/H265A
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit, kcat/Km is 52% of wild-type value
A249G/H265L
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit, kcat/Km is 63% of wild-type value
A249G/T354W
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit, kcat/Km is 26% of wild-type value
A293X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
A294G
-
mutation of the catalytical alpha-subunit, constructed mutant shows relaxed substrate specificity, efficient incorporation of p-iodo, p-ethynyl-, p-cyano-, and p-azidophenylalanines, but not p-acetylphenylalanine, into protein in the Escherichia coli host
A294G
-
mutant enzyme with A294G mutation in alpha-subunit, kcat/Km is 58% of wild-type value
A294G
-
thermosensitive active site mutant strain NP37 enzyme
A294G
-
thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
A294G
-
EcPheRS mutant
A294S
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
T251G
-
constructed mutant shows relaxed substrate specificity, efficient incorporation of p-acetylphenylalanine and reactive aryl ketones into protein in the Escherichia coli host
alphaDELTA1-175
Q9NSD9, Q9Y285
truncated N-terminal domain of the alpha subunit of hcPheRS
alphaDELTA60-170
Q9NSD9, Q9Y285
truncated N-terminal domain of the alpha subunit of hcPheRS
D325Y
-
the mutation is associated with early-onset epilepsy and isolated complex IV deficiency in muscle. The mutant is unable to bind ATP and shows consequently undetectable aminoacylation activity
N280S
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C/N280S
-
Ser57 and Asn280 map to positions away from the catalytic center and the anticodon binding domain of hmtPheRS, the mutant does not show significant loss in secondary structure or aminoacylation activity in vitro compared to wild-type enzyme. The S57C/N280S double mutant had remarkable stability even at low pH
A141W
O73984
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity
D234A
O73984
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
E127A
O73984
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
E219A
O73984
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
F145A
O73984
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
I216A
O73984
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
L168A
O73984
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
L202A
O73984
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
N217A
O73984
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity and shows abolished Tyr-tRNAPhe deacylation activity
Q126A
O73984
site-directed mutagenesis, the mutant shows reduced Tyr-tRNAPhe deacylation activity
R137A
O73984
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
R223A
O73984
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
S211A
O73984
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
T221A
O73984
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
T236A
O73984
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
Y189A
O73984
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
A333G
-
mtPheRS mutant
A450G
-
mutation in subunit alpha, tRNAPhe substrate specificity and flexibilty in charging pPhe variants compared to the wild-type enzyme
additional information
-
engineering of a mutated counter-selectable marker based on the Burkholderia pseudomallei PheS, i.e. the alpha-subunit of PheRS protein, effectiveness in three different transformed Burkholderia species, the mutant PheS protein effectively killed 100% of the bacteria in the presence of 0.1% 4-chlorophenylalanine, overview. Assembling of mutant pheS on several allelic replacement vectors, in addition to construction of selectable markers based on tellurite and trimethoprim resistance that are excisable by flanking unique FLP recombination target sequences, overview
A295X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
additional information
-
construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
additional information
-
editing-defective PheRS variants display significantly increased tyrosylation levels in the presence of EF-Tu, likely through elongation factor Tu, EF-Tu, protection of synthesized Tyr-tRNAPhe from hydrolysis, overview
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
A294G
Escherichia coli NP37
-
thermosensitive active site mutant strain NP37 enzyme, thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
-
additional information
Escherichia coli NP37
-
construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
-
K33C/T351C
-
mutant, crosslinked catalytic and RNA-binding domains, results in a closed form of mtPheRS that still catalyses ATP-dependent Phe activation, but is no longer able to transfer Phe to tRNA and complete the aminoacylation reaction
additional information
-
the N-terminal His-tag does not influence the kinetic parameters of tRNAPhe aminoacylation, cleavage of the His-tag by thrombin leads to nonspecific splitting of the enzyme that occurs in parallel to the main reaction
L210A
O73984
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
G458A
-
ctPheRS mutant
additional information
-
construction of enzyme mutants with better crystallization abilities, e.g. a PheRS variant which has both domains I and IV removed, or PheRS surface mutants, overview
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
design of an enzyme variant which incorporates aryl ketones into proteins
biotechnology
-
misacylation of suppressor tRNAPhe CUA by the PheRS mutant A294G with 4-iodo-L-phenylalanine might be useful in application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins, used for cell-free protein synthesis as a stoichiometric reagent, overview
biotechnology
Escherichia coli NP37
-
misacylation of suppressor tRNAPhe CUA by the PheRS mutant A294G with 4-iodo-L-phenylalanine might be useful in application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins, used for cell-free protein synthesis as a stoichiometric reagent, overview
-