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Literature summary for 3.1.26.4 extracted from

  • Hou, J.; Liu, Y.; Lu, Z.; Liu, X.; Liu, J.
    Biochemical characterization of RNase HII from Aeropyrum pernix (2012), Acta Biochim. Biophys. Sin. (Shanghai), 44, 339-346.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000361
-
5'-(6-carboxy-fluorescein)-cggagaugacgg-3'/5'-CCGTCTCTCCG-3' pH 9.0, 30°C Aeropyrum pernix

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the enzyme exhibits the highest activity in the presence of 5 mM Mn2+, 1 mM Co2+, or 10 mM Mg2+, respectively. The specific activity of the enzyme determined with 5 mM MnCl2 is slightly higher than that determined with 10 mM MgCl2, and about 2 folds higher than that determined with 1 mM CoCl2 Aeropyrum pernix
Mg2+ the enzyme exhibits the highest activity in the presence of 5 mM Mn2+, 1 mM Co2+, or 10 mM Mg2+, respectively. The specific activity of the enzyme determined with 5 mM MnCl2 is slightly higher than that determined with 10 mM MgCl2, and about 2 folds higher than that determined with 1 mM CoCl2 Aeropyrum pernix
Mn2+ the enzyme exhibits the highest activity in the presence of 5 mM Mn2+, 1 mM Co2+, or 10 mM Mg2+, respectively. The specific activity of the enzyme determined with 5 mM MnCl2 is slightly higher than that determined with 10 mM MgCl2, and about 2 folds higher than that determined with 1 mM CoCl2 Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YET5
-
-
Aeropyrum pernix DSM 11879 Q9YET5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-(6-carboxy-fluorescein)-cggagaugacgg-3'/5'-CCGTCTCTCCG-3' + H2O the enzyme cleaves 12-bp RNA/DNA at multiple sites between the 3rd and 11th residues, but most preferentially at c10–g11 and less preferentially at g5–a6 and u7–g8. The cleavage pattern of Mg2+-dependent activity is the same as that of Co2+-dependent activity, but different from that of Mn2+-dependent activity Aeropyrum pernix ?
-
?
5'-(6-carboxy-fluorescein)-cggagaugacgg-3'/5'-CCGTCTCTCCG-3' + H2O the enzyme cleaves 12-bp RNA/DNA at multiple sites between the 3rd and 11th residues, but most preferentially at c10–g11 and less preferentially at g5–a6 and u7–g8. The cleavage pattern of Mg2+-dependent activity is the same as that of Co2+-dependent activity, but different from that of Mn2+-dependent activity Aeropyrum pernix DSM 11879 ?
-
?

Synonyms

Synonyms Comment Organism
Ape-RNase HII
-
Aeropyrum pernix
RNase HII
-
Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Aeropyrum pernix
70
-
-
Aeropyrum pernix

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 90 50°C: about 60% of maximal activity, 90°C: about 40% of maximal activity Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
stabilization of the thermostable enzyme is enhanced with increased salt concentration (Mg2+ or K+) Aeropyrum pernix
70
-
fully stable at 70°C for at least 10 min under assay condition containing 100 mM MgCl2. Under the assay condition containing 10 mM MgCl2, little activity can be detected Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Aeropyrum pernix
11
-
-
Aeropyrum pernix