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Literature summary extracted from

  • Cazenave, C.; Frank, P.; Buesen, W.
    Characterization of ribonuclease H activities present in two cell-free protein synthesizing systems, the wheat germ extract and the rabbit reticulocyte lysate (1993), Biochimie, 75, 113-122.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.26.4 (NH4)2SO4 complete inhibition at 100 mM, in presence of 10 mM MgCl2 Oryctolagus cuniculus
3.1.26.4 (NH4)2SO4 moderate Triticum aestivum
3.1.26.4 NEM Mn2+-dependent activity is moderately sensitive, even at high concentrations Oryctolagus cuniculus
3.1.26.4 NEM Mg2+-dependent activity is highly sensitive Triticum aestivum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.4 Mg2+ required Triticum aestivum
3.1.26.4 Mg2+ enzyme is stimulated equally well by Mg2+, optimum concentration 5-10 mM, or Mn2+, optimum concentration 0.5-0.6 mM Oryctolagus cuniculus
3.1.26.4 Mn2+ enzyme is stimulated equally well by Mg2+, optimum concentration 5-10 mM, or Mn2+, optimum concentration 0.5-0.6 mM Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Oryctolagus cuniculus
-
-
-
3.1.26.4 Triticum aestivum
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.26.4 germ
-
 Triticum aestivum
-
3.1.26.4 reticulocyte
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.4 RNA-DNA hybrid + H2O
-
 Triticum aestivum ribonucleotide 5'-phosphomonoester
-
 ?
3.1.26.4 RNA-DNA hybrid + H2O
-
 Oryctolagus cuniculus ribonucleotide 5'-phosphomonoester
-
 ?