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Literature summary for 3.1.21.7 extracted from

  • Feng, H.; Klutz, A.; Cao, W.
    Active site plasticity of endonuclease V from Salmonella typhimurium (2005), Biochemistry, 44, 675-683.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
endonuclease V
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Salmonella enterica subsp. enterica serovar Typhimurium