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Literature summary for 3.1.26.3 extracted from

  • Sun, W.; Pertzev, A.; Nicholson, A.W.
    Catalytic mechanism of Escherichia coli ribonuclease III: kinetic and inhibitor evidence for the involvement of two magnesium ions in RNA phosphodiester hydrolysis (2005), Nucleic Acids Res., 33, 807-815.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxyisoquinoline-1,3-dione inhibits cleavage of R1.1 RNA, IC50: 0.014 mM for Mg2+-supported reaction, 0.008 mM for Mn2+-suppoeted reaction, noncompetitive inhibition Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent metal required, Mg2+ is the preffered species, evidennce for involvement of two Mg2+ ions in phosphodiester hydrolysis Escherichia coli
Mn2+ divalent metal required, Mn2+ can replace Mg2+ in activation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded RNA + H2O R1.1 RNA Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
RNase III
-
Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.014
-
inhibits cleavage of R1.1 RNA, IC50: 0.014 mM for Mg2+-supported reaction, 0.008 mM for Mn2+-suppoeted reaction, noncompetitive inhibition Escherichia coli 2-hydroxyisoquinoline-1,3-dione