Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.4 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

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

Metals/Ions

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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Triticum aestivum
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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