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Literature summary for 3.1.26.4 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
Search for more literature for 3.1.26.4

Protein Variants

Protein Variants Comment Organism
A115E mutation causes partially enhanced nuclease activity for the RNA-DNA duplex substrate, increase in its kcat of about 140% Pyrococcus furiosus
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
F114E mutations causes reduced nuclease activity for the RNA-DNA duplex substrate and reduced nuclease activity for the RNA-RNA duplex Pyrococcus furiosus
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U036
-
-
Pyrococcus horikoshii OT3 O59351
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNA-DNA heteroduplex + H2O the enzyme digests an RNA-RNA duplex in the presence of Mn2+ Pyrococcus furiosus ?
-
 ?
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

Synonyms Comment Organism
ribonuclease HII
-
 Pyrococcus furiosus
ribonuclease HII
-
 Pyrococcus horikoshii OT3

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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