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Literature summary for 3.1.21.7 extracted from

  • Wang, Y.; Zhang, L.; Zhu, X.; Li, Y.; Shi, H.; Oger, P.; Yang, Z.
    Biochemical characterization of a thermostable endonuclease V from the hyperthermophilic euryarchaeon Thermococcus barophilus Ch5 (2018), Int. J. Biol. Macromol., 117, 17-24 .
    View publication on PubMed
Search for more literature for 3.1.21.7

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
 Thermococcus barophilus
Co2+
-
 Thermococcus barophilus
NaCl activity is suppressed by high NaCl concentration. When adding 500 mM NaCl in the cleavage reaction, the cleavage efficiency of the enzyme is reduced to be approximately 50%. At NaCl concentrations over 800 mM, only slight endonuclease activity remains Thermococcus barophilus
Zn2+
-
 Thermococcus barophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal Thermococcus barophilus
Mn2+ a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal Thermococcus barophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + H2O Thermococcus barophilus endonuclease V is an important enzyme for repairing deoxyinosine in DNA ?
-
 ?
DNA + H2O Thermococcus barophilus Ch5 endonuclease V is an important enzyme for repairing deoxyinosine in DNA ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus barophilus A0A0S1X9V3
-
-
Thermococcus barophilus Ch5 A0A0S1X9V3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O endonuclease V is an important enzyme for repairing deoxyinosine in DNA Thermococcus barophilus ?
-
 ?
DNA + H2O the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA Thermococcus barophilus ?
-
 ?
DNA + H2O endonuclease V is an important enzyme for repairing deoxyinosine in DNA Thermococcus barophilus Ch5 ?
-
 ?
DNA + H2O the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA Thermococcus barophilus Ch5 ?
-
 ?

Synonyms

Synonyms Comment Organism
endo V
-
 Thermococcus barophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70 90
-
 Thermococcus barophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 the enzyme withstands 100°C for 120 min without significant loss of its activity Thermococcus barophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9
-
 Thermococcus barophilus

pH Range

pH Minimum pH Maximum Comment Organism
6 9 between pH 6.0 and pH 9.0, the enzyme exhibits more than 86% cleavage efficiency Thermococcus barophilus

General Information

General Information Comment Organism
physiological function endonuclease V is an important enzyme for repairing deoxyinosine in DNA Thermococcus barophilus