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Literature summary for 3.2.2.27 extracted from

  • Bogani, F.; Corredeira, I.; Fernandez, V.; Sattler, U.; Rutvisuttinunt, W.; Defais, M.; Boehmer, P.E.
    Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylase (2010), J. Biol. Chem., 285, 27664-27672.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
UL2 is cloned downstream of the CMV immediate-early promoter as a V5-tagged protein by inserting the UL2 open reading frame, amplified by PCR from HSV-1 strain KOS genomic DNA, into pcDNA3.1D/V5-His-TOPO, expression in Spodoptera frugiperda cells Human alphaherpesvirus 1

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information UL2 associates with the viral replisome. UL2 and the HSV-1 DNA polymerase catalytic subunit UL30 co-localize to viral prereplicative sites Human alphaherpesvirus 1
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Human alphaherpesvirus 1 viral uracil DNA glycosylase, UL2, in conjunction with the HSV-1 DNA polymerase catalytic subunit, UL30, cellular AP endonuclease and DNA ligase IIIalpha/XRCC1, perform uracil-initiated base excision repair. UL30 exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. UL2 and UL30 co-localize to viral prereplicative sites. The interaction between HSV-1 proteins UL2 and Pol occurs in HSV-1 infected cells ?
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?

Organism

Organism UniProt Comment Textmining
Human alphaherpesvirus 1
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HSV-1
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Purification (Commentary)

Purification (Comment) Organism
recombinant UL2 from Spodoptera frugiperda cells by gel filtration and two different steps of anion exchange chromatography Human alphaherpesvirus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information viral uracil DNA glycosylase, UL2, in conjunction with the HSV-1 DNA polymerase catalytic subunit, UL30, cellular AP endonuclease and DNA ligase IIIalpha/XRCC1, perform uracil-initiated base excision repair. UL30 exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. UL2 and UL30 co-localize to viral prereplicative sites. The interaction between HSV-1 proteins UL2 and Pol occurs in HSV-1 infected cells Human alphaherpesvirus 1 ?
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?
additional information cleavage of oligonucleotide PBAZ7 which contains a U at position 17 Human alphaherpesvirus 1 ?
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?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
physiological function base excision repair is required to maintain genome stability as a means to counter the accumulation of unusual bases and to protect from the loss of DNA bases Human alphaherpesvirus 1