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Literature summary for 2.7.7.8 extracted from

  • Chang, S.A.; Cozad, M.; Mackie, G.A.; Jones, G.H.
    Kinetics of polynucleotide phosphorylase: comparison of enzymes from Streptomyces and Escherichia coli and effects of nucleoside diphosphates (2008), J. Bacteriol., 190, 98-106.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Streptomyces coelicolor
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates has no effect on the phosphorolytic activity Escherichia coli ?
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additional information examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates results in decrease of Km value for phosphorolytic activity Streptomyces coelicolor ?
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