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Literature summary extracted from

  • Kargas, V.; Castro-Hartmann, P.; Escudero-Urquijo, N.; Dent, K.; Hilcenko, C.; Sailer, C.; Zisser, G.; Marques-Carvalho, M.J.; Pellegrino, S.; Wawiorka, L.; Freund, S.M.; Wagstaff, J.L.; Andreeva, A.; Faille, A.; Chen, E.; Stengel, F.; Bergler, H.; Warren, A.J.
    Mechanism of completion of peptidyltransferase centre assembly in eukaryotes (2019), eLife, 8, e44904 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.12 ribosome
-
Escherichia coli 5840
-
2.3.2.12 ribosome
-
Thermus thermophilus 5840
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 Escherichia coli
-
tRNA1 + peptidyl(aminoacyl-tRNA2)
-
?
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 Thermus thermophilus
-
tRNA1 + peptidyl(aminoacyl-tRNA2)
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.12 Escherichia coli
-
-
-
2.3.2.12 Thermus thermophilus Q5SHZ2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2
-
Escherichia coli tRNA1 + peptidyl(aminoacyl-tRNA2)
-
?
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2
-
Thermus thermophilus tRNA1 + peptidyl(aminoacyl-tRNA2)
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.12 ArfB
-
Escherichia coli
2.3.2.12 peptidyltransferase centre
-
Escherichia coli
2.3.2.12 peptidyltransferase centre
-
Thermus thermophilus
2.3.2.12 PTH
-
Thermus thermophilus

General Information

EC Number General Information Comment Organism
2.3.2.12 metabolism mechanism of peptidyltransferase centre (PTC) completion, overview. Requirement of the universally conserved Gly-Gly-Gln (GGQ) tripeptide in the highly conserved peptidyl transferase center suggesting that the reported conformation is likely shared during termination of protein synthesis in all domains of life Escherichia coli
2.3.2.12 metabolism mechanism of peptidyltransferase centre (PTC) completion, overview. Requirement of the universally conserved Gly-Gly-Gln (GGQ) tripeptide in the highly conserved peptidyl transferase center suggesting that the reported conformation is likely shared during termination of protein synthesis in all domains of life Thermus thermophilus
2.3.2.12 additional information the enzyme is part of the peptidyl transferase center (PTC), conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control, structure modeling, overview Escherichia coli
2.3.2.12 additional information the enzyme is part of the peptidyl transferase center (PTC), conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control, structure modeling, overview Thermus thermophilus