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Literature summary for 3.2.2.27 extracted from

  • Bogani, F.; Chua, C.N.; Boehmer, P.E.
    Reconstitution of uracil DNA glycosylase-initiated base excision repair in Herpes simplex virus-1 (2009), J. Biol. Chem., 284, 16784-16790.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
HSV-1 UL2 expression in Escherichia coli as a thioredoxin fusion protein Human alphaherpesvirus 1

Protein Variants

Protein Variants Comment Organism
additional information reconstitution of a system with purified HSV-1 and human proteins that perform all the steps of uracil DNA glycosylase-initiated base excision repair in Herpes simplex virus-1, including HSV-1 uracil DNA glycosylase, UL2, product analysis, overview Human alphaherpesvirus 1

Organism

Organism UniProt Comment Textmining
Human alphaherpesvirus 1
-
HSV-1
-
Human alphaherpesvirus 1 HSV-1
-
HSV-1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant thioredoxin fusion HSV-1 UL2 protein to homogeneity from Escherichia coli Human alphaherpesvirus 1

Synonyms

Synonyms Comment Organism
UL2
-
Human alphaherpesvirus 1
uracil DNA glycosylase
-
Human alphaherpesvirus 1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Human alphaherpesvirus 1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Human alphaherpesvirus 1