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Literature summary extracted from

  • Ioannou, M.; Coutsogeorgopoulos, C.; Drainas, D.
    Determination of eukaryotic peptidyltransferase activity by pseudo-first-order kinetic analysis (1997), Anal. Biochem., 247, 115-122.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.12 anisomycin inhibition of formation of AcPhe-puromycin catalyzed by rabbit reticulocyte ribosomes Oryctolagus cuniculus
2.3.2.12 blasticidin S inhibition of formation of Ac-Phe-puromycin catalyzed by rabbit reticulocyte ribosomes Oryctolagus cuniculus
2.3.2.12 sparsomycin inhibition of formation of AcPhe-puromycin catalyzed by rabbit reticulocyte ribosomes Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.12 ribosome 80S ribosomes Oryctolagus cuniculus 5840
-

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.12 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.12 blood salt-washed ribosomes Oryctolagus cuniculus
-
2.3.2.12 reticulocyte unwashed ribosomes Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.12 AcPhe-tRNA + puromycin AcPhe-tRNA-polyU-80S ribosome complex Oryctolagus cuniculus tRNA + AcPhe-puromycin
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.12 25
-
 enzyme assay, reaction in solution Oryctolagus cuniculus
2.3.2.12 37
-
 enzyme assay, disk reaction Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.2.12 0.0283
-
 AcPhe-tRNA reaction in solution Oryctolagus cuniculus
2.3.2.12 0.0483
-
 AcPhe-tRNA disk reaction Oryctolagus cuniculus