Organism | UniProt | Comment | Textmining |
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Salmonella enterica subsp. enterica serovar Typhimurium | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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DNA + H2O | limited turnover on cleavage of deoxyinosine- and xanthosine-containing DNA. Nicking activity is similar between the double-stranded deoxyinosine- and deoxyxanthosine-containing DNA. Endonuclease V can only turnover deoxyuridine-containing DNA to a limited extent when substrate is in excess. Endonuclease V achieves tight binding to deoxyuridine-containing DNA. The active site of salmonella endonuclease V can accomodate pyrimidine-containing mismatches, resulting in more comparable cleavage of pyrimidine- and purine-containing mismatches. The plastic nature of the active site allows the enzyme to enfold both purine and pyrimidine deaminated lesions or base pair mismatches | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
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DNA + H2O | limited turnover on cleavage of deoxyinosine- and xanthosine-containing DNA. Nicking activity is similar between the double-stranded deoxyinosine- and deoxyxanthosine-containing DNA. Endonuclease V can only turnover deoxyuridine-containing DNA to a limited extent when substrate is in excess. Endonuclease V achieves tight binding to deoxyuridine-containing DNA. The active site of salmonella endonuclease V can accomodate pyrimidine-containing mismatches, resulting in more comparable cleavage of pyrimidine- and purine-containing mismatches. The plastic nature of the active site allows the enzyme to enfold both purine and pyrimidine deaminated lesions or base pair mismatches | Salmonella enterica subsp. enterica serovar Typhimurium 14028 | ? | - |
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Synonyms | Comment | Organism |
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endonuclease V | - |
Salmonella enterica subsp. enterica serovar Typhimurium |