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Literature summary for 3.1.30.2 extracted from

  • Romanova, J.; Gubskaya, V.; Nuretdinov, I.; Zainutdinova, E.; Filimonova, M.
    Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease (2017), BioNanoSci., 7, 276-283 .
No PubMed abstract available
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 DNA at the optimal Mg2+ amount, both the Km and the Kcat values are similar to both RNA and DNA substrates Serratia marcescens
additional information
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 RNA at the optimal Mg2+ amount, both the Km and the Kcat values are similar to both RNA and DNA substrates Serratia marcescens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ in the presence of 0.58 mM Mg2+, the digestive activity of the enzyme is approximately fourfold increased as compared with the activity in the absence of Mg2+ taken as 100%. Further fivefold increase in Mg2+ concentration causes near 1.5fold enhancement in the enzyme activity. Subsequent two- and fourfold increases in Mg2+ concentration have only a minor impact on the enzyme activity within the experimental error range. 6.0-11.6 mM of Mg2+ corresponding to 20-40 Mg2+ per 1 phosphate in RNA is optimal for the hydrolysis of RNA. Optimal Mg2+ amount is linked with the changing secondary structure of RNA substrates within A-helix. Addition of Mg2+ affects both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that is supported by strong increase in the Kcat values and change in the Km values Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens P13717
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O in absence of Mg2+ the enzyme shows a preference for DNA as compared to RNA Serratia marcescens ?
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RNA + H2O in absence of Mg2+ the enzyme shows a preference for DNA as compared to RNA Serratia marcescens ?
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