Literature summary for 4.2.99.B1 extracted from

Bogani, F.; Boehmer, P.E.
The replicative DNA polymerase of herpes simplex virus 1 exhibits apurinic/apyrimidinic and 5-deoxyribose phosphate lyase activities (2008), Proc. Natl. Acad. Sci. USA, 105, 11709-11714.

Search for more literature for 4.2.99.B1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Spodoptera friguperda	Human alphaherpesvirus 1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0018	-	mimic of a preincised DNA duplex with a 5'dRP at the site of the nick	pH 7.5, 37°C	Human alphaherpesvirus 1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
EDTA	1 mM in enzyme assay	Human alphaherpesvirus 1
additional information	independent of Mg2+	Human alphaherpesvirus 1

Organism

Organism	UniProt	Comment	Textmining
Human alphaherpesvirus 1	-	a large dsDNA virus that encodes its own DNA replication machinery	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein, copurification with DNA polymerase, proved by analytical gel filtration	Human alphaherpesvirus 1

Reaction

Reaction	Comment	Organism	Reaction ID
catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site	enzyme cleaves 3' to apurinic/apyrimidinic sites and is capable of removing 5' dRP residues at sites that mimic preincision with AP endonuclease. The activity of UL30 on the preincised and nicked substrates ist significantly greater than observed on apurinic/apyrimidinic DNA. These activities are integral to base excision repair and lead to DNA cleavage on 3' side on abasic sites and 5'-dRP residues that remain after cleavage by 5'-AP endonuclease, via beta-elimination forming a Schiff base intermediate	Human alphaherpesvirus 1	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
mimic of a preincised DNA duplex with a 5'dRP at the site of the nick	nick substrate, containing a 3'-[32P]-labelled 16-mer with a terminal 5'-uracil, which upon pretreatment with uracil-DNA glycosylase is converted to an oligonuceotide with a 5' dRP residue, having a electrophoretic mobility of a 14.5-mer	Human alphaherpesvirus 1	14-mer-oligonucleotide + 2-deoxy-D-ribose 5-phosphate	removal of 5'dRP generates a 3'-[32P]-labelled 14-mer	?
additional information	no reaction with a DNA substrate possessing 5' uracil flap	Human alphaherpesvirus 1	?	-	?
preincised DNA duplex with a 5'dRP flap	flap substrate, containing a 3'-[32P]-labelled 16-mer that possesses a 5' uracil flap, which upon pretreatment with uracil-DNA glycosylase is converted to an oligonuceotide with a 5' dRP flap, having a electrophoretic mobility of a 15.5-mer	Human alphaherpesvirus 1	15-mer-oligonucleotide + 2-deoxy-D-ribose 5-phosphate	the removal of the 5' dRP generates a 3'-[32P]-labelled 15-mer	?

Subunits

Subunits	Comment	Organism
More	the catalytic subunit of the HSV-1 DNA polymerase exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities	Human alphaherpesvirus 1

Synonyms

Synonyms	Comment	Organism
5' dRP lyase	-	Human alphaherpesvirus 1
5'-deoxyribose phosphate lyase	-	Human alphaherpesvirus 1
HSV-1 Pol	-	Human alphaherpesvirus 1
HSV-1-DNA polymerase	catalytic subunit	Human alphaherpesvirus 1
UL30	-	Human alphaherpesvirus 1

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0075	-	mimic of a preincised DNA duplex with a 5'dRP at the site of the nick	pH 7.5, 37°C	Human alphaherpesvirus 1

pH Optimum

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

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Release 2023.1 (January 2023)