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Literature summary for 6.1.1.20 extracted from

  • Stepanov, V.G.; Moor, N.A.; Ankilova, V.N.; Vasil'eva, I.A.; Sukhanova, M.V.; Lavrik, O.I.
    A peculiarity of the reaction of tRNA aminoacylation catalyzed by phenylalanyl-tRNA synthetase from the extreme thermophile Thermus thermophilus (1998), Biochim. Biophys. Acta, 1386, 1-15.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the rate of overcharging of the tRNAPhe is dependenton the buffer system used Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
AMP
-
Thermus thermophilus
diphosphate
-
Thermus thermophilus
additional information the rate of overcharging of the tRNAPhe is dependenton the buffer system used Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe Thermus thermophilus
-
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir
ATP + L-phenylalanine + tRNAPhe Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.21
-
purified enzyme, 37°C Thermus thermophilus
0.31
-
purified recombinant enzyme expressed in Escherichia coli, 37°C Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2 L-phenylalanine + tRNAPhe mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging Thermus thermophilus AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe overcharged product cannot be isolated from living cells ir
ATP + 2 L-phenylalanine + tRNAPhe mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe overcharged product cannot be isolated from living cells ir
ATP + L-phenylalanine + tRNAPhe
-
Thermus thermophilus AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir
ATP + L-phenylalanine + tRNAPhe tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human Thermus thermophilus AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir
ATP + L-phenylalanine + tRNAPhe
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir
ATP + L-phenylalanine + tRNAPhe tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
ir

Synonyms

Synonyms Comment Organism
CML33
-
Thermus thermophilus
FRS
-
Thermus thermophilus
HSPC173
-
Thermus thermophilus
L-Phenylalanyl-tRNA synthetase
-
Thermus thermophilus
Phenylalanine translase
-
Thermus thermophilus
Phenylalanine--tRNA ligase
-
Thermus thermophilus
Phenylalanine-tRNA synthetase
-
Thermus thermophilus
Phenylalanyl transfer ribonucleic acid synthetase
-
Thermus thermophilus
Phenylalanyl-transfer ribonucleate synthetase
-
Thermus thermophilus
Phenylalanyl-transfer RNA ligase
-
Thermus thermophilus
Phenylalanyl-transfer RNA synthetase
-
Thermus thermophilus
Phenylalanyl-tRNA ligase
-
Thermus thermophilus
Phenylalanyl-tRNA synthetase
-
Thermus thermophilus
PheRS
-
Thermus thermophilus
Synthetase, phenylalanyl-transfer ribonucleate
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Thermus thermophilus