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Literature summary for 3.1.21.7 extracted from

  • Mi, R.; Abole, A.; Cao, W.
    Dissecting endonuclease and exonuclease activities in endonuclease V from Thermotoga maritima (2011), Nucleic Acids Res., 39, 536-544.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.21.7

Protein Variants

Protein Variants Comment Organism
D43A active site mutant, exhibits minimal non-specific activity Thermotoga maritima
H116T DNA and Mn2+ binding defective enzyme mutant Thermotoga maritima
H214D the enzyme mutant is defective in non-specific nuclease activity Thermotoga maritima
H214E active site mutant, exhibits minimal non-specific activity Thermotoga maritima
additional information construction of enzyme mutants defective in DNA binding and Mn2+ as a metal cofactor. The majority of the binding defective mutants show varying degrees of non-specific activities Thermotoga maritima
Q20A DNA and Mn2+ binding defective enzyme mutant Thermotoga maritima
R118A DNA and Mn2+ binding defective enzyme mutant Thermotoga maritima
R205K DNA and Mn2+ binding defective enzyme mutant Thermotoga maritima

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermotoga maritima endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. But Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity and non-specific 5'-exonuclease activity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. But Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity and non-specific 5'-exonuclease activity Thermotoga maritima ?
-
 ?
additional information cleavage of 50-labeled inosine- and non-inosine-containing substrates Thermotoga maritima ?
-
 ?

Synonyms

Synonyms Comment Organism
endonuclease V
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 Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 assay at Thermotoga maritima

pH Range

pH Minimum pH Maximum Comment Organism
7.4
-
 assay at Thermotoga maritima

General Information

General Information Comment Organism
physiological function endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion Thermotoga maritima