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Literature summary extracted from

  • Kitamura, S.; Fujishima, K.; Sato, A.; Tsuchiya, D.; Tomita, M.; Kanai, A.
    Characterization of RNase HII substrate recognition using RNase HII-argonaute chimaeric enzymes from Pyrococcus furiosus (2010), Biochem. J., 426, 337-344 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.4 A115E mutation causes partially enhanced nuclease activity for the RNA-DNA duplex substrate, increase in its kcat of about 140% Pyrococcus furiosus
3.1.26.4 D110T mutation causes loss of nuclease activity for the RNA–RNA duplex, nuclease activity for the RNA-DNA duplex substrate is similar to wild-type activity Pyrococcus furiosus
3.1.26.4 F114E mutations causes reduced nuclease activity for the RNA-DNA duplex substrate and reduced nuclease activity for the RNA-RNA duplex Pyrococcus furiosus
3.1.26.4 R113E mutations causes partially reduced nuclease activity for the RNA-DNA duplex substrate and reduced nuclease activity for the RNA-RNA duplex Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.26.4 0.12
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme F114E Pyrococcus furiosus
3.1.26.4 0.12
-
 RNA-DNA heteroduplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mg2+ Pyrococcus furiosus
3.1.26.4 0.12
-
 RNA-DNA heteroduplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+ Pyrococcus furiosus
3.1.26.4 0.14
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme A115E Pyrococcus furiosus
3.1.26.4 0.2
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme R113E Pyrococcus furiosus
3.1.26.4 1.3
-
 RNA-RNA duplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+ Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.4 Mg2+ activates reaction with RNA-DNA heteroduplex and RNA-RNA duplex Pyrococcus furiosus
3.1.26.4 Mn2+ the enzyme digests an RNA-RNA duplex in the presence of Mn2+, no activity in presence of Mg2+ Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Pyrococcus furiosus Q8U036
-
-
3.1.26.4 Pyrococcus horikoshii OT3 O59351
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.4 recombinant RNase HII and mutant proteins Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.4 RNA-DNA heteroduplex + H2O the enzyme digests an RNA-RNA duplex in the presence of Mn2+ Pyrococcus furiosus ?
-
 ?
3.1.26.4 RNA-RNA duplex + H2O weak activity. Amino acid residues Asp110, Arg113 and Phe114 of RNase HII are strongly involved in the dsRNA-digestion activity of the enzyme Pyrococcus furiosus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.26.4 ribonuclease HII
-
 Pyrococcus furiosus
3.1.26.4 ribonuclease HII
-
 Pyrococcus horikoshii OT3

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.4 50
-
 assay at Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.26.4 0.093
-
 RNA-RNA duplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+ Pyrococcus furiosus
3.1.26.4 0.41
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme F114E Pyrococcus furiosus
3.1.26.4 6.6
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme R113E Pyrococcus furiosus
3.1.26.4 11.3
-
 RNA-DNA heteroduplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+ Pyrococcus furiosus
3.1.26.4 15.3
-
 RNA-DNA heteroduplex 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme A115E Pyrococcus furiosus
3.1.26.4 17
-
 RNA-DNA heteroduplex 50°C, pH 8.0, wild-type enzyme, divalent cation: Mg2+ Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.4 8
-
 assay at Pyrococcus furiosus