Characterization of cytosol phosphopeptides

50 S subunits of E. coli ribosomes catalyze the reaction of the 2'(3')-N-(formyl) methionine ester of adenosine 5'-phosphate and Phe-tRNA resulting in peptide bond synthesis. Cytidine 5'-phosphate stimulates this process on 50 S ribosomal subunits as well as on intact ribosomes. The obtained data show that the areas of the peptidyltransferase donor site which binds the 3'-terminal fragment of peptidyl-tRNA possess completely formed structures on 50 S ribosomal subunits.

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Catalysis of the peptide bond formation by 50 S subunits of E. Coli ribosomes with N-(formyl) methionine ester of adenylic acid as peptide donor

Kotusov

Kukhanova

Krayevsky

et al. 1976

Mol Biol Rep

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Further characterization of mitochondrial protein phosphatase

Clari

Donella

Pinna

et al. 1975

Archives of Biochemistry and Biophysics

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Structural requirements for the enzymatic phosphorylation of phosvitin

Pinna

Donella

Clari

et al. 1975

Biochimica et Biophysica Acta (BBA) - Enzymology

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Characterization of cytosol phosphopeptides

Cited by 5 publications

References 11 publications

Catalysis of the peptide bond formation by 50 S subunits of E. Coli ribosomes with N-(formyl) methionine ester of adenylic acid as peptide donor

Catalysis of the peptide bond formation by 50 S subunits of E. Coli ribosomes with N-(formyl) methionine ester of adenylic acid as peptide donor

Further characterization of mitochondrial protein phosphatase

Structural requirements for the enzymatic phosphorylation of phosvitin

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