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Literature summary for 4.6.1.18 extracted from

  • Kulms, D.; Schäfer, G.; Hahn, U.
    SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties. (1995), Biochem. Biophys. Res. Commun., 214, 646-652.
    View publication on PubMed
Search for more literature for 4.6.1.18

General Stability

General Stability Organism
enzyme is resistant to unfolding by 8 M urea. It can only be unfolded by guanidinium chloride at high concentrations or by a combinantion of acid and thermally induced denaturation Sulfolobus acidocaldarius

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no effect of bivalent cations on enzyme Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius
-
 enzyme exhibits RNase activity as well as DNA-binding properties
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.52
-
 pH 7.0, 65°C Sulfolobus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5S rRNA + H2O
-
 Sulfolobus acidocaldarius 3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Sulfolobus acidocaldarius

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
 stable up to Sulfolobus acidocaldarius

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
 Sulfolobus acidocaldarius

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
 enzyme is very stable near neutral pH values Sulfolobus acidocaldarius