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Literature summary extracted from

  • Sandigursky, M.; Franklin, W.
    Thermostable uracil-DNA glycosylase from Thermotoga maritima, a member of a novel class of DNA repair enzymes (1999), Curr. Biol., 9, 531-534 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.27 expression in Escherichia coli Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.27 Thermotoga maritima Q9WYY1
-
-
3.2.2.27 Thermotoga maritima DSM 3109 Q9WYY1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.27
-
Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.27 additional information the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil Thermotoga maritima ?
-
?
3.2.2.27 additional information the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil Thermotoga maritima DSM 3109 ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.2.27 75
-
stable up to Thermotoga maritima

General Information

EC Number General Information Comment Organism
3.2.2.27 metabolism the enzyme removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway Thermotoga maritima