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Information on EC 3.2.2.23 - DNA-formamidopyrimidine glycosylase and Organism(s) Escherichia coli and UniProt Accession P50465
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3.2.2.23 DNA-formamidopyrimidine glycosylaseIUBMB Comments
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
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Word Map
- 3.2.2.23
- strand
- comet
- glycosylases
-
genotoxic
- purine
-
single-stranded
-
abasic
- duplex
-
fpg-sensitive
- thymine
-
excises
- 7,8-dihydro-8-oxoguanine
- ape1
-
ring-opened
- 8-oxo-7,8-dihydroguanine
-
8-oxodg
- endonucleases
-
8-oxo-7,8-dihydro-2'-deoxyguanosine
- 5-hydroxyuracil
-
micronucleus
-
transversions
-
neils
-
alkali-labile
-
biomonitoring
-
3-methyladenine-dna
- mispairs
-
interstrand
-
lesion-specific
- spiroiminodihydantoin
- bromate
- medicine
- 2'-deoxyguanosine
-
klenow
- ap-endonuclease
-
uvrabc
-
miscoding
-
base-excision
-
apurinic
- 8-oxo-2'-deoxyguanosine
-
monoadducts
- dihydrouracil
-
enzyme-modified
-
unhook
-
mutyh
-
endoiii
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
neil1, neil3, fpg protein, formamidopyrimidine-dna glycosylase, formamidopyrimidine dna glycosylase, 8-oxoguanine-dna glycosylase, formamidopyrimidine glycosylase, fapy-dna glycosylase, fpg-1, fpg-l, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase
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2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase
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2,6-diamino-4-hydroxy-5N-methyl-formamidopyrimidine-DNA glycosylase
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8-hydroxyguanine endonuclease
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8-oxoguanine DNA glycosylase
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deoxyribonucleate glycosidase
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DNA glycohydrolase (releasing 2,6-diamino-4-hydroxy-5-(N-methyl)-formamidopyrimidine)
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Fapy-DNA glycosylase
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formamidopyrimidine DNA glycosylase
formamidopyrimidine-DNA glycosyl hydrolase
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formamidopyrimidine-DNA glycosylase
FPG
Fpg protein
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glycosidase, deoxyribonucleate formamidopyrimidine
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MutM
additional information
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Fpg belongs to the class of DNA glycosylases/abasic site lyases
formamidopyrimidine DNA glycosylase
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formamidopyrimidine-DNA glycosylase
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FPG
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FPG
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MutM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
mechanism
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hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
reaction mechanism
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hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
kinetic mechanism
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hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
catalytic mechanism
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
several fast sequential conformational changes occur in enzyme after binding to its substrate, converting the protein into a catalytically active conformation
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
formation of the transition state complex from the reactants exhibits an overall free energy of 9.6 kcal/mol
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
the damaged base is first destabilized by the enzyme binding and then everted from DNA, followed by insertion of several amino acid residues into DNA and isomerization of the enzyme into a pre-excision complex
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
chemical reaction mechanism, overview. For the catalysis to occur, the damaged base must be extruded from the DNA helix and placed in the active site of enzyme, this is achieved in Fpg by kinking DNA at the lesion point. The reaction mechanism involves coupled conformational changes in the enzyme and DNA, which proceed sequentially and assemble the catalytic groups in the active site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
CAS REGISTRY NUMBER
COMMENTARY
78783-53-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA containing 2'-deoxy-8-oxonebularine residues + H2O
?
23mer oligonucleotide containing a single site, very poor substrate
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
FapyGua
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
FapyAde
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
23-oligomer
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
-
-
-
-
?
23mer oligonucleotide duplex containing 8-oxoguanine + H2O
8-oxoguanine + oligonucleotide
-
-
-
?
53mer containing 8-oxoguanine + H2O
53mer with an abasic site + 8-oxoguanine
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
DNA containing 2,6-diamino-4-hydroxyformamidopyrimidine residues + H2O
2,6-diamino-4-hydroxyformamidopyrimidine + DNA
-
repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
DNA containing 5,6-dihydrothymine residues + H2O
?
-
dublex 33mer oligonucleotide, poor substrate
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine + H2O
?
-
double-stranded oligonucleotides, N-glycosylase/beta,delta-elimination reaction
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
5-hydroxycytosine + DNA
-
-
-
-
?
DNA containing 5-hydroxyuracil residues + H2O
5-hydroxyuracil + DNA
-
-
-
-
?
DNA containing 7,8-dihydro-8-oxoguanine residues + H2O
DNA + 7,8-dihydro-8-oxoguanine
-
-
-
-
?
DNA containing 7-deaza-2'-deoxyguanosine + H2O
7-deaza-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 7-methyl-7-deazaguanine residues + H2O
7-methyl-7-deazaguanine + DNA
-
-
-
-
?
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine + H2O
7-methyl-8-oxo-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 8-hydroxyadenine residues + H2O
8-hydroxyadenine + DNA
-
poor substrate
-
-
?
DNA containing 8-oxo-2'-deoxyguanosine + H2O
8-oxo-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 8-oxo-7,8-dihydroguanine residues + H2O
DNA + 8-hydroxyguanine
-
-
-
-
?
DNA containing 8-oxo-7,8-dihydroguanine residues + H2O
DNA + 8-oxo-7,8-dihydroguanine
-
-
-
?
DNA containing 8-oxo-guanine residues mispaired to adenine + H2O
DNA + 8-oxoguanine
-
-
-
-
?
DNA containing 8-oxo-guanine residues mispaired to guanine + H2O
DNA + 8-oxoguanine
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-
-
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?
DNA containing 8-oxo-guanine residues mispaired to thymine + H2O
DNA + 8-oxoguanine
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?
DNA containing 8-oxoguanine opposite A + H2O
8-oxoguanine + DNA
poor substrate, analysis of rate constants of conformational transitions
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-
?
DNA containing 8-oxoguanine opposite C + H2O
8-oxoguanine + DNA
good substrate, analysis of rate constants of conformational transitions
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-
?
DNA containing 8-oxoguanine opposite G + H2O
8-oxoguanine + DNA
analysis of rate constants of conformational transitions
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-
?
DNA containing 8-oxoguanine opposite T + H2O
8-oxoguanine + DNA
analysis of rate constants of conformational transitions
-
-
?
DNA containing 8-thio-2'-deoxyguanosine + H2O
8-thio-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing formamidopyrimidine-guanine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
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-
-
?
DNA containing guanidinohydantoin + H2O
guanidinohydantoin + DNA
-
for DNA duplex length of 30 bp, the excision efficiency in pairs with C, G, or T is similar to 8-oxoguanine. Opposite A, the base removal activity is more efficient than removal of 8-oxoguanine
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-
?
DNA containing methylated formamidopyrimidine-guanine residues + H2O
2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine + DNA
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-
-
?
DNA containing ring-opened N7-methylguanine + H2O
2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine + DNA
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA
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-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
DNA containing spiroiminodihydantoin + H2O
spiroiminodihydantoin + DNA
-
for DNA duplex length of 30 bp, the excision efficiency in pairs with C, G, or T is similar to 8-oxoguanine. Opposite A, the base removal activity is more efficient than removal of 8-oxoguanine
-
-
?
DNA containing tetrahydrofuran residues + H2O
tetrahydrofuran + DNA
-
-
-
-
?
oligonucleotide containing 8-oxo-2'-deoxyguanosine residue + H2O
oligonucleotide + 8-oxo-2'-deoxyguanosine
-
-
-
-
?
oligonucleotide containing abasic site residue + H2O
oligonucleotide + abasic site
-
-
-
-
?
oligonucleotide containing tetrahydrofuran residue + H2O
oligonucleotide + tetrahydrofuran
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-
-
-
?
DNA + H2O
?
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
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-
?
DNA + H2O
?
removes oxidized purines from oxidatively damaged DNA
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-
?
DNA + H2O
?
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
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-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
24-oligomer, Lys-155 directly interacts with the C8 oxygen of 8-oxopurines involving proton transfer or transient formation of an ion pair between enzyme and substrate, mechanism
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?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
DNA glycosylase/AP lyase activity
-
?
13mer oligonucleotide duplex containing 8-oxoguanine + H2O
8-oxoguanine + oligonucleotide
-
-
-
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?
13mer oligonucleotide duplex containing 8-oxoguanine + H2O
8-oxoguanine + oligonucleotide
-
-
-
?
DNA + H2O
?
-
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
-
-
?
DNA + H2O
?
-
role of Lys-155 for substrate binding and product release, AP lyase mechanism
-
-
?
DNA + H2O
?
-
FpG-DNA interactions establish contacts with DNA ligands, which span no more than 9 base-pairs, structural studies of Fpg-DNA complexes
-
-
?
DNA + H2O
?
-
excises oxidized purines from damaged DNA, Schiff base intermediate, enzyme structure, bilobal protein with a wide, positive charged DNA-binding groove and a helix-2-turn-helix motif that participates in DNA binding, damage recognition, catalytic mechanism
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-
?
DNA + H2O
?
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
-
catalytic mechanism involves formation of Schiff base intermediate between DNA containing an oxidized residue and the N-terminal Pro-2 of Fpg, mendatory role of P-2 in 7,8-dihydro-8-oxoguanine-DNA glycosylase and AP lyase activity, but less in 2,6-diamino-4-hydroxy-5-N-methyl-formamidopyrimidine-DNA glycosylase activity
-
-
?
DNA + H2O
?
-
active site is located within the first 73 amino acids of the N-terminus
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-
?
DNA + H2O
?
-
excises purine bases with ring-opened imidazoles, associated activity that nicks DNA at apurinic/apyrimidinic sites, mechanism of cleavage involves beta elimination
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?
DNA + H2O
?
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
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-
?
DNA + H2O
?
-
enzyme catalyzes the nicking of both the phosphodiester bonds 3' and 5' of apurinic or apyrimidinic sites in DNA so that the base-free deoxyribose is replaced by a gap limited by 3'-phosphate and 5'-phosphate ends, the 2 nickings are not the result of hydrolytic processes, the enzyme rather catalyzes a beta-elimination reaction immediately followed by a delta-elimination
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-
?
DNA + H2O
?
-
DNA repair enzyme specific for the removal of purine-derived lesions from DNA damaged by free radicals and other oxidative processes
-
-
?
DNA + H2O
?
-
plays an important role in base excision repair of oxidatively damaged DNA
-
-
?
DNA + H2O
?
-
involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
-
removal with similar specificity as 4,6-diamino-5-formamidopyrimidine and 8-hydroxyguanine
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
-
FapyGua
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
-
FapyGua
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
-
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
-
removal with similar specificity as 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 8-hydroxyguanine
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
-
FapyAde
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
-
FapyAde
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
-
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
-
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
?
-
double-stranded oligonucleotides containing 5-hydroxy-2'-deoxycytidine, N-glycosylase/beta,delta-elimination reaction
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
?
-
dublex 33mer oligonucleotide, excision mechanism
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
-
dublex, primary physiological substrate, DNA repair
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
-
-
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
-
the C-8 keto group of 8-oxodeoxyguanine and the carbonyl moiety of formamidopyrimidine enable the enzyme to recognize and bind duplex DNA containing modified bases
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
-
mechanism involving protonation at O-6 of 8-oxodeoxyguanine
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
-
dublex 20-oligomer, catalytic mechanism with enzyme-substrate Schiff base intermediate, amino terminal localization of the catalytic site, C-8 keto group of 8-oxodeoxyguanine plays a critical role in binding enzyme
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
-
kinetic mechanism, 3 activities: DNA-glycosylase, beta-elimination/AP-lyase and delta elimination, 12-nucleotide dublex containing 8-oxo-G in the sixth position of one strand, conformational transitions of Fpg protein during the catalytic process
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
-
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
DNA glycosylase/AP lyase activity
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
34mer oligonucleotide containing a single 7,8-dihydro-8-oxoguanine residue
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
dublex oligodeoxynucleotides containing 8-oxo-7,8-dihydro-2-deoxyguanosine positioned opposite dC, dG or dT are cleaved, but not opposite dA or single-stranded DNA, cleaves 3 and 5 to the modified base
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
comparison of repair activities of human OGG1 and Escherichia coli Fpg, enzymes show distinct preferences for the base opposite 8-oxoguanine, mechanism via Schiff base intermediate
treatment of 7,8-dihydro-8-oxoguanine with Fpg results in delta-elimination products
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
mendatory role of P-2 in 7,8-dihydro-8-oxoguanine-DNA glycosylase activity
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
7,8-dihydro-8-oxo-2-deoxyguanosine, natural substrate, substrate recognition, mechanism
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
readily incises dublexes with cytosine, thymine or guanine opposite, but much slower with adenine opposite 7,8-dihydro-8-oxoguanine, 2 activities: DNA-glycosylase and DNA nicking at abasic sites
treatment of 7,8-dihydro-8-oxoguanine with Fpg results in delta-elimination products
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
7,8-dihydro-8-oxoguanine opposite C dublex DNA, formation of a Schiff base intermediate, important role for Lys-57 in the 7,8-dihydro-8-oxoG-DNA glycolase activity in vitro and in vivo
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
7,8-dihydro-8-oxoguanine-DNA
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
7,8-dihydro-8-oxoguanine-DNA
treatment of 7,8-dihydro-8-oxoguanine with Fpg results in delta-elimination products
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
removal with similar specificity as 4,6-diamino-5-formamidopyrimidine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, important role of Lys-57 in Fpg activity for 8-hydroxyguanine, but lesser significant role for formamidopyrimidines, Pro-2 is critical for substrate recognition and in catalysis of its excision
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
54 nt DNA oligomer, CoFpg and ZnFpg are equally active at cleaving the DNA at the site of the oxidized guanine
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species
-
-
?
DNA containing 8-oxoguanine residues + H2O
8-oxoguanine + DNA
-
8-oxoguanine residues opposite cytosine
-
-
?
DNA containing 8-oxoguanine residues + H2O
DNA + 8-oxoguanine
best substrate
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
enzyme excises the secondary alkylation product of 7-methylguanine Fapy
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
double-stranded DNA is preferred to single-stranded DNA
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
dublex oligodeoxynucleotides containing Me-Fapy
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
comparison of repair activities of human OGG1 and Escherichia coli Fpg, almost no paired base-dependent repair, effect of sequence context on repair efficiency, mechanism via Schiff base intermediate
treatment of me-Fapy with Fpg results in delta-elimination products
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
less mendatory role of P-2 in 2,6-diamino-4-hydroxy-5-N-methyl-formamidopyrimidine-DNA glycosylase activity
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
the C-8 keto group of 8-oxodeoxyguanine and the carbonyl moiety of formamidopyrimidine enable the enzyme to recognize and bind duplex DNA containing modified bases, mechanism
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
amino terminal localization of the catalytic site
-
?
additional information
?
-
-
not: carbocyclic substrate analog of 8-oxo-7,8-dihydro-2-deoxyguanosine
-
-
?
additional information
?
-
-
no cleavage of 3-methyladenine, uracil, intact 7-methylguanine from DNA
-
-
?
additional information
?
-
-
not: dublex DNA containing a single tetrahydrofuran residue
-
-
?
additional information
?
-
-
human OGG1 and Escherichia coli Fpg are structurally unrelated enzymes with different catalytic residues, OGG1: Lys-249 and Asp-268 in the hairpin-helix-hairpin-GDP motif are involved in the glycosylase/AP lyase activity, Fpg: uses a proline residue in the N-terminal region for catalysis
-
-
?
additional information
?
-
-
not: DNA containing 8-oxo-7,8-dihydro-2-deoxyadenosine, single-stranded DNA, dublex DNA containing synthetic abasic sites, mismatches containing dG, unmodified DNA
-
-
?
additional information
?
-
-
base excision repair initiated by the enzyme is less effective in the first two days of growth and more effective later in stationary phase
-
-
?
additional information
?
-
-
enzyme mediates repair of lesions containing hydantoins in vivo
-
-
?
additional information
?
-
-
cross-linking of active center with a series of reactive oligonucleotide duplexes containing both a single 8-oxoguanine residue and an O-ethyl-substituted diphosphate internucleotide group results in identification of seven phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L56 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
-
-
?
additional information
?
-
-
defective repair of 5-hydroxy-2-deoxycytidine in Cockayne syndrome cells is complementated by Escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III
-
-
?
additional information
?
-
-
formamidopyrimidine-DNA N-glycosylase operates in the base excision repair pathway in bacteria by removing oxidized guanine bases from DNA and can also cleave the nascent or preformed abasic DNA by beta,delta-elimination. The cleaved product formation is initially reversible
-
-
?
additional information
?
-
-
FPG excises oxidatively damaged purines in the base excision repair pathway, overview
-
-
?
additional information
?
-
-
formamidopyrimidine-DNA N-glycosylase removes oxidized guanine bases from DNA. The cleaved product formation is initially reversible, it is followed by conformational changes in the enzyme and DNA molecules that represent the postchemical irreversible rate-limiting steps. The overall rate-limiting step of the enzymatic reaction seems to be the release of Fpg from its adduct with the 4-oxo-2-pentenal remnant of the deoxyribose moiety formed as a result of DNA strand cleavage by beta,delta-elmination, the initial chemical steps are fast and reversible. Catalytic mechanism, overview
-
-
?
additional information
?
-
-
FPG excises oxidatively damaged purines in the base excision repair pathway, it acts on DNA containing 5,6-dihydrouracil, 8-oxo-7,8-dihydroguanine, or on apurinic/apyrimidinic DNA base pairs, analysis of conformational dynamics of Fpg protein and DNA substrates, rate constants of conformational transitions, and intrinsic mechanism of recognition and excision of damaged bases in DNA, overview
-
-
?
additional information
?
-
-
formamidopyrimidine DNA glycosylase is specific for oxidized purines
-
-
?
additional information
?
-
-
the enzyme is more active towards oxidized purines than oxidized pyrimidines and has little to no activity toward DNA containing thymine glycols and osmium-tetroxide-treated DNA
-
-
?
additional information
?
-
-
analysis of acidity and proton affinity for a range of substrates such as 8-oxoguanine, 8-oxoadenine, 8-oxoinosine, 8-oxonebularine, formamidopyrimidine-guanine, 5-hydroxyuracil, and 5,6-dihydrothymine. The most favorable mechanism involves preprotonation of the O4', which results in the opening of the ribose ring
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
-
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxyformamidopyrimidine residues + H2O
2,6-diamino-4-hydroxyformamidopyrimidine + DNA
-
repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species
-
-
?
DNA containing ring-opened N7-methylguanine + H2O
2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine + DNA
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA
-
-
?
DNA + H2O
?
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
-
DNA repair enzyme specific for the removal of purine-derived lesions from DNA damaged by free radicals and other oxidative processes
-
-
?
DNA + H2O
?
-
plays an important role in base excision repair of oxidatively damaged DNA
-
-
?
DNA + H2O
?
-
involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
-
dublex, primary physiological substrate, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
-
repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species
-
-
?
DNA containing 8-oxoguanine residues + H2O
DNA + 8-oxoguanine
best substrate
-
-
?
additional information
?
-
-
base excision repair initiated by the enzyme is less effective in the first two days of growth and more effective later in stationary phase
-
-
?
additional information
?
-
-
enzyme mediates repair of lesions containing hydantoins in vivo
-
-
?
additional information
?
-
-
defective repair of 5-hydroxy-2-deoxycytidine in Cockayne syndrome cells is complementated by Escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III
-
-
?
additional information
?
-
-
formamidopyrimidine-DNA N-glycosylase operates in the base excision repair pathway in bacteria by removing oxidized guanine bases from DNA and can also cleave the nascent or preformed abasic DNA by beta,delta-elimination. The cleaved product formation is initially reversible
-
-
?
additional information
?
-
-
FPG excises oxidatively damaged purines in the base excision repair pathway, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
Zn2+
Zn2+
-
zinc(II)- and cobalt(II)-associated enzyme, metal-binding domain, zinc-associated motif is located at the C-terminus and essential for damaged DNA recognition
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by 1.2 mM 8-oxo-7,8-dihydro-2-deoxyguanosine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000009
DNA
pH 7.5, 20°C, 24-oligomer DNA containing apurinic/apyrimidinic sites, lyase activity, K155A mutant Fpg
0.000019
DNA
pH 7.5, 20°C, 24-oligomer DNA containing AP sites, lyase activity, wild-type Fpg
0.0000069
DNA containing 7-hydro-8-oxoguanine residues
pH 7.5, 37°C, 24-oligomer, wild-type Fpg
-
0.0000075
DNA containing 7-hydro-8-oxoguanine residues
pH 7.5, 37°C, 24-oligomer, K155A mutant Fpg
-
0.000023
DNA containing ring-opened N7-methylguanine residues
pH 7.5, 37°C, 23-oligomer, wild-type Fpg
-
0.000029
DNA containing ring-opened N7-methylguanine residues
pH 7.5, 37°C, 23-oligomer, K155A mutant Fpg
-
0.0000039
13mer oligonucleotide duplex containing 8-oxoguanine
mutant R244E, pH 7.5, 37°C
-
0.0000047
13mer oligonucleotide duplex containing 8-oxoguanine
mutant S208A, pH 7.5, 37°C
-
0.000006
13mer oligonucleotide duplex containing 8-oxoguanine
mutant Q234R, pH 7.5, 37°C
-
0.0000081
13mer oligonucleotide duplex containing 8-oxoguanine
wild-type, pH 7.5, 37°C
-
0.0000088
13mer oligonucleotide duplex containing 8-oxoguanine
mutant Q234R/R244E, pH 7.5, 37°C
-
0.0000063
23mer oligonucleotide duplex containing 8-oxoguanine
mutant R258Q, pH 7.5, 30°C
-
0.0000081
23mer oligonucleotide duplex containing 8-oxoguanine
wild-type, pH 7.5, 30°C
-
0.0000081
23mer oligonucleotide duplex containing 8-oxoguanine
mutant N168Q, pH 7.5, 30°C
-
0.000018
23mer oligonucleotide duplex containing 8-oxoguanine
mutant R108K, pH 7.5, 30°C
-
0.00178
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57R mutant Fpg, from DNA gamma-irradiated under NO2
-
0.00187
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57G mutant Fpg, from DNA gamma-irradiated under NO2
-
0.00343 - 0.00376
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37°C, wild-type Fpg
-
0.00422
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57G mutant Fpg, from DNA treated with H2O2/Fe(III)-EDTA/asc
-
0.00487
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57R mutant Fpg, from DNA treated with H2O2/Fe(III)-EDTA/asc
-
0.00078 - 0.00084
DNA containing 4,6-diamino-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57G mutant Fpg
-
0.00079 - 0.0009
DNA containing 4,6-diamino-5-formamidopyrimidine residues
-
pH 7.4, 37°C, K57R mutant Fpg
-
0.00107 - 0.00129
DNA containing 4,6-diamino-5-formamidopyrimidine residues
-
pH 7.4, 37°C, wild-type Fpg
-
0.000004
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37°C, 34-oligomer, wild-type and K57R mutant Fpg
-
0.000008
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37°C, 34-oligomer, K57G mutant Fpg
-
0.000008
DNA containing 8-hydroxyguanine residues
-
pH 7.5, 20°C, dublex DNA containing a single 8-oxoguanine residue positioned opposite dC
-
0.00093 - 0.00155
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37°C, K57R mutant Fpg
-
0.00109
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37°C, wild-type Fpg, from DNA treated with H2O2/Fe(III)-EDTA/asc
-
0.00126
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37°C, K57G mutant Fpg
-
0.00311
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37°C, wild-type Fpg, from DNA gamma-irradiated under NO2
-
0.022
DNA containing 8-oxo-guanine residues mispaired to adenine
-
wild-type
-
0.023
DNA containing 8-oxo-guanine residues mispaired to adenine
-
mutant R108A
-
0.0001
DNA containing 8-oxo-guanine residues mispaired to guanine
-
wild-type
-
0.0051
DNA containing 8-oxo-guanine residues mispaired to guanine
-
mutant R108A
-
0.00019
DNA containing 8-oxo-guanine residues mispaired to thymine
-
wild-type
-
0.0042
DNA containing 8-oxo-guanine residues mispaired to thymine
-
mutant R108A
-
0.000009 - 0.000011
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37°C, wild-type, K57G and K57R mutant Fpg
-
0.000038
DNA containing ring-opened N7-methylguanine residues
-
pH 7.5, 37°C
-
0.000041
DNA containing ring-opened N7-methylguanine residues
-
pH 7.5, 20°C, dublex DNA containing a single Me-Fapy residue positioned opposite dC
-
additional information
additional information
-
thermodynamic characterization of Fpg binding to lesion-containing 13mer DNA dublexes, binding affinity
-
additional information
additional information
-
Km for DNA substrate is affected by the base opposite the lesion
-
additional information
additional information
-
kinetic parameters of duplex oligonucleotides and mismatched duplexes
-
additional information
additional information
-
kinetics, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00167
DNA containing 8-hyroxyguanine
-
pH 7.8, 37°C, 34-oligomer, K57R mutant Fpg
-
additional information
additional information
-
turnover of duplex oligonucleotides and mismatched duplexes
-
0.0568
DNA
pH 7.5, 20°C, 24-oligomer DNA containing AP sites, lyase activity, wild-type Fpg
0.0883
DNA
pH 7.5, 20°C, 24-oligomer DNA containing AP sites, lyase activity, K155A mutant Fpg
0.000383
DNA containing 7-hydro-8-oxoguanine residues
pH 7.5, 37°C, 24-oligomer, K155A mutant Fpg
-
0.0185
DNA containing 7-hydro-8-oxoguanine residues
pH 7.5, 37°C, 24-oligomer, wild-type Fpg
-
0.0012
DNA containing ring-opened N7-methylguanine residues
pH 7.5, 37°C, 23-oligomer, K155A mutant Fpg
-
0.00383
DNA containing ring-opened N7-methylguanine residues
pH 7.5, 37°C, 23-oligomer, wild-type Fpg
-
0.0065
13mer oligonucleotide duplex containing 8-oxoguanine
mutant R244E, pH 7.5, 37°C
-
0.0133
13mer oligonucleotide duplex containing 8-oxoguanine
mutant S208A, pH 7.5, 37°C
-
0.0148
13mer oligonucleotide duplex containing 8-oxoguanine
mutant Q234R/R244E, pH 7.5, 37°C
-
0.0153
13mer oligonucleotide duplex containing 8-oxoguanine
mutant Q234R, pH 7.5, 37°C
-
0.0283
13mer oligonucleotide duplex containing 8-oxoguanine
wild-type, pH 7.5, 37°C
-
0.07
23mer oligonucleotide duplex containing 8-oxoguanine
mutant R108K, pH 7.5, 30°C
-
0.08
23mer oligonucleotide duplex containing 8-oxoguanine
mutant R258Q, pH 7.5, 30°C
-
0.16
23mer oligonucleotide duplex containing 8-oxoguanine
mutant N168Q, pH 7.5, 30°C
-
1.7
23mer oligonucleotide duplex containing 8-oxoguanine
wild-type, pH 7.5, 30°C
-
0.000167
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37°C, 34-oligomer, K57G mutant Fpg
-
0.00717
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37°C, 34-oligomer, wild-type Fpg
-
0.000075
DNA containing 8-oxo-guanine residues mispaired to adenine
-
mutant R108A
-
0.00011
DNA containing 8-oxo-guanine residues mispaired to adenine
-
wild-type
-
0.00038
DNA containing 8-oxo-guanine residues mispaired to guanine
-
mutant R108A
-
0.0035
DNA containing 8-oxo-guanine residues mispaired to guanine
-
wild-type
-
0.0003
DNA containing 8-oxo-guanine residues mispaired to thymine
-
mutant R108A
-
0.0047
DNA containing 8-oxo-guanine residues mispaired to thymine
-
wild-type
-
0.002
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37°C, K57G and K57R mutant Fpg
-
0.00833
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37°C, wild-type Fpg
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
with increase in dublex length of nonspecific ds 8-23mer oligonucleotides, Ki values decrease from 0.05 mM to 0.0007 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.054
polymeric DNA containing ring-opened N7-methylguanine residues as substrate, wild-type Fpg
additional information
additional information
molecular modeling and molecular dynamics simulation to interprete substrate discrimination in the active site
additional information
-
molecular modeling and molecular dynamics simulation to interprete substrate discrimination in the active site
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
DNA glycosylases play a key role in the base excision repair pathway, Fpg belongs to the class of DNA glycosylases/abasic site lyases excising several oxidatively damaged purines in the base excision repair pathway
physiological function
physiological function
-
the enzyme is nonrendundant and required for the rapid global repair of oxidized purine and pyrimidine damage in vivo. In vivo, the enzyme is required for the rapid removal its substrate lesions as well as a significant fraction of those recognized by endonuclease III, from the chromosome
physiological function
-
the enzyme repairs both oxidized bases and different types of bulky DNA adducts
physiological function
Fpg selectively facilitates eversion of 8-oxoguanine by stabilizing several intermediate states, helping the rapidly sliding enzyme avoid full extrusion of every encountered base for interrogation
physiological function
nucleoid-associated protein HU enhances the 8-oxoguanine-DNA glycosylase activity of Fpg by facilitating the release of the enzyme from its final DNA product. The displacement of Fpg from its end-DNA product by HU is an active mechanism in which HU recognizes the product when it is still bound by Fpg. The two proteins form a transient ternary complex Fpg/DNA/HU which results in the release of Fpg and the molecular entrapment of single-strand breaks by HU
physiological function
protein displays three conserved polar bridges (Arg54-Glu131, Gln234-Arg244, and Tyr170-Ser208) located in functional regions of the protein. The coevolving pairs do not form isolated bridges but rather participate in tight local clusters of hydrogen bonds. The Arg54-Glu131 bridge, connecting the N- and C-terminal domains, is important for DNA binding. Mutations of the Gln234-Arg244 bridge, located at the base of the single Fpg beta-hairpin zinc finger, do not affect the activity but sharply decreases the melting temperature of the protein, with the bridge reversal partially restoring the thermal stability
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
30200
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cross-linking of active center with a series of reactive oligonucleotide duplexes containing both a single 8-oxoguanine residue and an O-ethyl-substituted diphosphate internucleotide group results in identification of seven phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L56 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
additional information
-
Fpg consists of two domains connected by a hinge polypeptide. The N-terminal domain contains a beta-sandwich core and a long alpha-helix with an N-terminal catalytic dyad, proline-glutamate. The C-terminal domain is mostly alpha-helical, containing two motifs almost universally conserved in Fpg proteins: a helix-two turn-helix motif and a beta-hairpin Cys4 zinc finger. The protein molecule possesses a positively charged cleft where damaged DNA is bound
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMR spectroscopy study of enzyme free in solution and bound to a double-stranded DNA oligomer containing 1,3-propanediol. Enzyme is a very dynamic molecule even after binding to damaged DNA
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K155A
mutant with 50fold decreased activity with 7-hydro-8-oxoguanine-DNA as substrate, only 3-4fold decreased activity with 7-methylformamidopyrimidine-DNA, increased AP lyase activity
E173Q
no enzymic activity, E173 may play a crucial role in forming the active site pocket
E2Q
no enzymic activity, interactions with G167 and Y170 are interupted
E3Q
-
inactive. Mutant binds DNA duplexes containing spiroiminodihydantoin or guanidinohydantoin about 1000fold more tightly over corresponding duplexes containing 8-oxoguanine
F110A
-
the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps
F110W
-
the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps
F111A
-
the mutant displays a significant increase in the average diffusion constant compared to the wild-type protein with no enzymatic activity on DNA containing 8-oxoguanine residues opposite cytosine. The mutant has little or no ability to form a Schiff base with 8-oxoguanine residues opposite cytosine or 5,6-dihydrouracil opposite guanine compared to wild type enzyme
H71A
severely compromised in turnover of oligonucleotides with 8-oxoguanosine opposie cytosine, but show turnover rates comparable to wild-type on abasic-site containing DNA
K155A
K57A
-
mutant with about 15% of wild-type activity in both N-glycosylase and AP lyase activity
K57G
K57R
P2E
P2G
P2T
-
mutant with 10% of wild-type 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA glycosylase activity and barely detectable 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no cleavage of DNA containing AP sites
S208A
mutation has no effect, in both wild-type and S208 A residue Tyr170 quickly reorients to form an alternative set of hydrogen bonds
Y170F
mutation decreases Fpg binding but does not fully inactivate the protein
additional information
K155A
-
effect of mutation on specificity, mutant with very low activity, kinetic study
K155A
-
mutant with reduced 8-oxoguanine-DNA but unchanged Fapy-DNA glycosylase activity
K155A
-
mutant enzyme with decreased N-glycosylase and increased AP lyase activity, it dissociates prematurely from the covalent enzyme-DNA complex leading to a higher turnover number for DNA containing an AP site
K57G
-
study of the effect of the mutation on the structure dynamics, mutant with decreased 8-hydroxyguanine-DNA glycosylase activity
K57G
-
mutant has dramatically reduced 7,8-dihydro-8-oxoguanine-DNA glycosylase activity and is poorly effective in formation of Schiff base complex with 8-oxoG/C, little effect on 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine-DNA glycosylase activity, no effect on DNA nicking activity at abasic sites
K57G
-
effect of mutation on specificity, mutant removes FapyAde and FapyGua with reduced activity compared to wild-type Fpg, kinetic study
K57R
-
effect of mutation on specificity, mutant removes FapyAde and FapyGua with reduced activity compared to wild-type Fpg, kinetic study
K57R
-
slight effect of mutation on 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no effect on 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine-DNA glycosylase activity and on DNA nicking activity at abasic sites
P2E
-
study of the effect of the mutation on the structure dynamics, mutation causes complete loss of DNA glycosylase/beta-lyase activity and induces a conformational change leading to a more rigid globular structure than wild-type, K57G and P2G Fpg
P2E
-
completely inactive mutant: no 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA/7,8-dihydro-8-oxoguanine-DNA glycosylase activity or cleavage of DNA containing AP sites
P2G
-
effect of mutation on specificity, mutant with very low activity, kinetic study
P2G
-
study of the effect of the mutation on the structure dynamics, mutant with complete loss of beta-lyase and partial loss of DNA glycosylase activity
P2G
-
mutant with 10% of wild-type 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA glycosylase activity and barely detectable 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no cleavage of DNA containing AP sites
additional information
-
expression in Chinese hamster ovary cells results in decrease of the levels of oxypurine clustered damages while those of oxypyrimidine clusters and abasic clusters are unchanged. Growth rates of cells are increased and the level of spontaneous background mutants in the hypoxanthine guanine phosphoribosyl transferase gene is decreased
additional information
-
expression of enzyme in human cells from patients belonging to Cockayne syndrome complementation groups A and B completely corrects the repair deficiency in both CS-A and CS-B cells. The sensitivity of CS-B cells to elevated concentrations of potassium bromate is not compensated by expression of enzyme
additional information
-
expression of enzyme-green fluorescent protein fusion protein in human bladder cells. Cells expressing the fusion protein repair 8-oxoguanine and abasic sites at accelerated rates and are resistant to the oxidizing carcinogen potassium bromate
additional information
-
monitoring of spontaneous revertants in a background in which a T/G replacement inactivates the lacZ gene, in strains possessing and lacking Fpg activity. In strains without enzymic activity grown on glucose medium, the proportion of revertants increases over a 5-day period. In contrast, in strains with enzymic activity, revertants appear primarily during the first 2-3 days after plating, few new revertants appear in the following days
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39
54
65
-
free protein undergoes irreversible thermal unfolding with a Tm of about 65°C
additional information
-
purified enzyme is very sensitive to extreme temperature fluctuations
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
15N-labeled formamidopyrimidine DNA glycosylase is as active as unlabeled enzyme
-
50% glycerol destabilizes during storage, concentration of above 10% cause a 60% reduction in activity
-
complete loss of activity if the enzyme stored at -20°C or -80°C is subsequently thawed for assaying
-
rapid loss of activity when a conventional pressure cell is used to concentrate enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and K155A mutant Fpg, expressed in Escherichia coli BLR(DE3)
DE52 resin column chromatography and HPLC-Shodex carboxymethyl cellulose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of K155A mutant and wild-type Fpg in Escherichia coli BL21(DE3) and BLR(DE3)
expression of EGFP-tagged enzyme in HEK-293T cells. Transformation of primary human fibroblasts of a Cockayne syndrome patient using SV40, expression of FPG in 5-hydroxy-2'-deoxycytidine repair defective human cells complements the disorder and leads to stable correction of the delayed removal of both oxidized purines and oxidized pyrimidines in the cells, detailed overview
-
fpg structural gene is cloned and sequenced, overexpression in Escherichia coli HB101
-
P2E, P2T and P2G mutant Fpg are cloned and expressed in Escherichia coli BH20(fpg-)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
comparison of human Ogg1, Escherichia coli Fpg and endonuclease III for the ability to modify the sensitivity of the comet assay. All three endonucleases recognize oxidative DNA damage and, in addition, Fpg and endonuclease III also recognize alkylation damage. Use of human Ogg1 in the modified comet assay offers a useful alternative to Fpg and is more specific for 8-oxoguanine and methyl-fapy-guanine
medicine
medicine
-
expression of enzyme in human cells from patients belonging to Cockayne syndrome complementation groups A and B completely corrects the repair deficiency in both CS-A and CS-B cells. The sensitivity of CS-B cells to elevated concentrations of potassium bromate is not compensated by expression of enzyme
medicine
-
expression of enzyme-green fluorescent protein fusion protein in human bladder cells. Cells expressing the fusion protein repair 8-oxoguanine and abasic sites at accelerated rates and are resistant to the oxidizing carcinogen potassium bromate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boiteux, S.; O'Connor, T.R.; Laval, J.
Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein
EMBO J.
6
3177-3183
1987
Escherichia coli, Escherichia coli HB1100
Tchou, J.; Grollman, A.P.
The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site
J. Biol. Chem.
270
11671-11677
1995
Escherichia coli, Escherichia coli JM109
Tchou, J.; Bodepudi, V.; Shibutani, S.; Antoshechkin, I.; Miller, J.; Grollman, A.P.; Johnson, F.
Substrate specificity of Fpg protein. Recognition and cleavage of oxidatively damaged DNA
J. Biol. Chem.
269
15318-15324
1994
Escherichia coli
Tchou, J.; Kasai, H.; Chung, M.H.; Laval, J.; Grollman, A.P.; Nishimura, S.
8-Oxoguanine (8-hydroxyguanine) DNA glycosylase and its substrate specificity
Proc. Natl. Acad. Sci. USA
88
4690-4694
1991
Escherichia coli
O'Connor, T.R.; Laval, J.
Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites
Proc. Natl. Acad. Sci. USA
86
5222-5226
1989
Escherichia coli
Bailly, V.; Verly, W.G.; O'Connor, T.; Laval, J.
Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine]DNA glycosylase
Biochem. J.
262
581-589
1989
Escherichia coli
Chetsanga, C.J.; Lozon, M.; Makaroff, C.; Savage, L.
Purification and characterization of Escherichia coli formamidopyrimidine-DNA glycosylase that excises damaged 7-methylguanine from deoxyribonucleic acid
Biochemistry
20
5201-5207
1981
Escherichia coli
Hatahet, Z.; Kow, Y.W.; Purmal, A.A.; Cunningham, R.P.; Wallace, S.S.
New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase
J. Biol. Chem.
269
18814-18820
1994
Escherichia coli
Gilboa, R.; Zharkov, D.O.; Golan, G.; Fernandes, A.S.; Gerchman, S.E.; Matz, E.; Kycia, J.H.; Grollman, A.P.; Shoham, G.
Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA
J. Biol. Chem.
277
19811-19816
2002
Escherichia coli
Buchko, G.W.; Hess, N.J.; Bandaru, V.; Wallace, S.S.; Kennedy, M.A.
Spectroscopic studies of zinc(II)- and cobalt(II)-associated Escherichia coli formamidopyrimidine-DNA glycosylase: extended X-ray absorption fine structure evidence for a metal-binding domain
Biochemistry
39
12441-12449
2000
Escherichia coli
Kuznetsov, S.V.; Sidorkina, O.M.; Jurado, J.; Bazin, M.; Tauc, P.; Brochon, J.C.; Laval, J.; Santus, R.
Effect of single mutations on the structural dynamics of a DNA repair enzyme, the Escherichia coli formamidopyrimidine-DNA glycosylase. A fluorescence study using tryptophan residues as reporter groups
Eur. J. Biochem.
253
413-420
1998
Escherichia coli, Escherichia coli BH20
Sidorkina, O.; Dizdaroglu, M.; Laval, J.
Effect of single mutations on the specificity of Escherichia coli FPG protein for excision of purine lesions from DNA damaged by free radicals
Free Radic. Biol. Med.
31
816-823
2001
Escherichia coli
Rabow, L.E.; Kow, Y.W.
Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis
Biochemistry
36
5084-5096
1997
Escherichia coli (P50465), Escherichia coli
Rabow, L.; Venkataraman, R.; Kow, Y.W.
Mechanism of action of Escherichia coli formamidopyrimidine N-glycosylase: Role of K155 in substrate binding and product release
Prog. Nucleic Acid Res. Mol. Biol.
68
223-234
2001
Escherichia coli
D'Ham, C.; Romieu, A.; Jaquinod, M.; Gasparutto, D.; Cadet, J.
Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins: Kinetic and mechanistic aspects
Biochemistry
38
3335-3344
1999
Escherichia coli
Sidorkina, O.M.; Laval, J.
Role of lysine-57 in the catalytic activities of Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg protein)
Nucleic Acids Res.
26
5351-5357
1998
Escherichia coli, Escherichia coli BH20
Minetti, C.A.S.A.; Remeta, D.P.; Zharkov, D.O.; Plum, G.E.; Johnson, F.; Grollman, A.P.; Breslauer, K.J.
Energetics of lesion recognition by a DNA repair protein: Thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes
J. Mol. Biol.
328
1047-1060
2003
Escherichia coli, Escherichia coli B834 (DE3)
Fedorova, O.S.; Nevinsky, G.A.; Koval, V.V.; Ishchenko, A.A.; Vasilenko, N.L.; Douglas, K.T.
Stopped-flow kinetic studies of the interaction between Escherichia coli Fpg protein and DNA substrates
Biochemistry
41
1520-1528
2002
Escherichia coli
Asagoshi, K.; Yamada, T.; Terato, H.; Ohyama, Y.; Monden, Y.; Arai, T.; Nishimura, S.; Aburatani, H.; Lindahl, T.; Ide, H.
Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine
J. Biol. Chem.
275
4956-4964
2000
Escherichia coli
Sidorkina, O.M.; Laval, J.
Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein
J. Biol. Chem.
275
9924-9929
2000
Escherichia coli
Perlow-Poehnelt, R.A.; Zharkov, D.O.; Grollman, A.P.; Broyde, S.
Substrate discrimination by formamidopyrimidine-DNA glycosylase: distinguishing interactions within the active site
Biochemistry
43
16092-16105
2004
Escherichia coli (P05523), Escherichia coli
Buchko, G.W.; McAteer, K.; Wallace, S.S.; Kennedy, M.A.
Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface
DNA Repair
4
327-339
2005
Escherichia coli
Zaika, E.I.; Perlow, R.A.; Matz, E.; Broyde, S.; Gilboa, R.; Grollman, A.P.; Zharkov, D.O.
Substrate discrimination by formamidopyrimidine-DNA glycosylase: a mutational analysis
J. Biol. Chem.
279
4849-4861
2004
Escherichia coli
Koval, V.V.; Kuznetsov, N.A.; Zharkov, D.O.; Ishchenko, A.A.; Douglas, K.T.; Nevinsky, G.A.; Fedorova, O.S.
Pre-steady-state kinetics shows differences in processing of various DNA lesions by Escherichia coli formamidopyrimidine-DNA glycosylase
Nucleic Acids Res.
32
926-935
2004
Escherichia coli
Reddy, P.; Jaruga, P.; O'Connor, T.; Rodriguez, H.; Dizdaroglu, M.
Overexpression and rapid purification of Escherichia coli formamidopyrimidine-DNA glycosylase
Protein Expr. Purif.
34
126-133
2004
Escherichia coli
Harbut, M.B.; Meador, M.; Dodson, M.L.; Lloyd, R.S.
Modulation of the turnover of formamidopyrimidine DNA glycosylase
Biochemistry
45
7341-7346
2006
Escherichia coli (P05523), Escherichia coli
Kuznetsov, N.A.; Koval, V.V.; Zharkov, D.O.; Vorobjev, Y.N.; Nevinsky, G.A.; Douglas, K.T.; Fedorova, O.S.
Pre-steady-state kinetic study of substrate specificity of Escherichia coli formamidopyrimidine--DNA glycosylase
Biochemistry
46
424-435
2007
Escherichia coli (P05523), Escherichia coli
Krishnamurthy, N.; Muller, J.G.; Burrows, C.J.; David, S.S.
Unusual structural features of hydantoin lesions translate into efficient recognition by Escherichia coli Fpg
Biochemistry
46
9355-9365
2007
Escherichia coli
Paul, S.; Gros, L.; Laval, J.; Sutherland, B.M.
Expression of the E. coli fpg protein in CHO cells lowers endogenous oxypurine clustered damage levels and decreases accumulation of endogenous Hprt mutations
Environ. Mol. Mutagen.
47
311-319
2006
Escherichia coli
Ropolo, M.; Degan, P.; Foresta, M.; DErrico, M.; Lasiglie, D.; Dogliotti, E.; Casartelli, G.; Zupo, S.; Poggi, A.; Frosina, G.
Complementation of the oxidatively damaged DNA repair defect in Cockayne syndrome A and B cells by Escherichia coli formamidopyrimidine DNA glycosylase
Free Radic. Biol. Med.
42
1807-1817
2007
Escherichia coli
Ropolo, M.; Geroldi, A.; Degan, P.; Andreotti, V.; Zupo, S.; Poggi, A.; Reed, A.; Kelley, M.R.; Frosina, G.
Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein
Int. J. Cancer
118
1628-1634
2006
Escherichia coli
Hamm, M.L.; Gill, T.J.; Nicolson, S.C.; Summers, M.R.
Substrate specificity of Fpg (MutM) and hOGG1, two repair glycosylases
J. Am. Chem. Soc.
129
7724-7725
2007
Escherichia coli, Homo sapiens
Rogacheva, M.; Ishchenko, A.; Saparbaev, M.; Kuznetsova, S.; Ogryzko, V.
High resolution characterization of formamidopyrimidine-DNA glycosylase interaction with its substrate by chemical cross-linking and mass spectrometry using substrate analogs
J. Biol. Chem.
281
32353-32365
2006
Escherichia coli, Homo sapiens
Smith, C.C.; ODonovan, M.R.; Martin, E.A.
hOGG1 recognizes oxidative damage using the comet assay with greater specificity than FPG or ENDOIII
Mutagenesis
21
185-190
2006
Escherichia coli, Homo sapiens
Shu, J.; Schellhorn, H.E.; Murphy, T.M.
Stationary phase-induction of G->T mutations in Escherichia coli
Mutat. Res.
596
106-112
2006
Escherichia coli
Minetti, C.A.; Remeta, D.P.; Breslauer, K.J.
A continuous hyperchromicity assay to characterize the kinetics and thermodynamics of DNA lesion recognition and base excision
Proc. Natl. Acad. Sci. USA
105
70-75
2008
Escherichia coli
Kuznetsov, N.A.; Zharkov, D.O.; Koval, V.V.; Buckle, M.; Fedorova, O.S.
Reversible chemical step and rate-limiting enzyme regeneration in the reaction catalyzed by formamidopyrimidine-DNA glycosylase
Biochemistry
48
11335-11343
2009
Escherichia coli
Foresta, M.; Ropolo, M.; Degan, P.; Pettinati, I.; Kow, Y.W.; Damonte, G.; Poggi, A.; Frosina, G.
Defective repair of 5-hydroxy-2-deoxycytidine in Cockayne syndrome cells and its complementation by Escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III
Free Radic. Biol. Med.
48
681-690
2010
Escherichia coli
Koval, V.V.; Kuznetsov, N.A.; Ishchenko, A.A.; Saparbaev, M.K.; Fedorova, O.S.
Real-time studies of conformational dynamics of the repair enzyme E. coli formamidopyrimidine-DNA glycosylase and its DNA complexes during catalytic cycle
Mutat. Res.
685
3-10
2010
Escherichia coli
Schalow, B.J.; Courcelle, C.T.; Courcelle, J.
Escherichia coli Fpg glycosylase is nonrendundant and required for the rapid global repair of oxidized purine and pyrimidine damage in vivo
J. Mol. Biol.
410
183-193
2011
Escherichia coli, Escherichia coli SR108
Dunn, A.R.; Kad, N.M.; Nelson, S.R.; Warshaw, D.M.; Wallace, S.S.
Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA
Nucleic Acids Res.
39
7487-7498
2011
Escherichia coli
Reddy, P.T.; Jaruga, P.; Nelson, B.C.; Lowenthal, M.; Dizdaroglu, M.
Stable isotope-labeling of DNA repair proteins, and their purification and characterization
Protein Expr. Purif.
78
94-101
2011
Escherichia coli
Rana, J.; Huang, H.
Actions of the Klenow fragment of DNA polymerase I and some DNA glycosylases on chemically stable analogues of N7-methyl-2-deoxyguanosine
Bioorg. Med. Chem.
21
6886-6892
2013
Escherichia coli
Kain, J.; Karlsson, H.L.; Moeller, L.
DNA damage induced by micro- and nanoparticles - interaction with FPG influences the detection of DNA oxidation in the comet assay
Mutagenesis
27
491-500
2012
Escherichia coli
Kuznetsov, N.A.; Vorobjev, Y.N.; Krasnoperov, L.N.; Fedorova, O.S.
Thermodynamics of the multi-stage DNA lesion recognition and repair by formamidopyrimidine-DNA glycosylase using pyrrolocytosine fluorescence--stopped-flow pre-steady-state kinetics
Nucleic Acids Res.
40
7384-7392
2012
Escherichia coli
Foresta, M.; Izzotti, A.; La Maestra, S.; Micale, R.; Poggi, A.; Vecchio, D.; Frosina, G.
Accelerated repair and reduced mutagenicity of DNA damage induced by cigarette smoke in human bronchial cells transfected with E.coli formamidopyrimidine DNA glycosylase
PLoS ONE
9
e87984
2014
Escherichia coli
Prakash, A.; Doublie, S.; Wallace, S.S.
The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage
Prog. Mol. Biol. Transl. Sci.
110
71-91
2012
Escherichia coli (P05523), Geobacillus stearothermophilus (P84131), Lactococcus lactis (P42371), Thermus thermophilus (O50606), Thermus thermophilus DSM 579 (O50606)
Le Meur, R.; Culard, F.; Nadan, V.; Goffinont, S.; Coste, F.; Guerin, M.; Loth, K.; Landon, C.; Castaing, B.
The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase
Biochem. J.
471
13-23
2015
Escherichia coli (P05523)
Kiruba, G.S.; Xu, J.; Zelikson, V.; Lee, J.K.
Gas-phase studies of formamidopyrimidine glycosylase (Fpg) substrates
Chemistry
22
3881-3890
2016
Escherichia coli
Endutkin, A.V.; Koptelov, S.S.; Popov, A.V.; Torgasheva, N.A.; Lomzov, A.A.; Tsygankova, A.R.; Skiba, T.V.; Afonnikov, D.A.; Zharkov, D.O.
Residue coevolution reveals functionally important intramolecular interactions in formamidopyrimidine-DNA glycosylase
DNA Repair
69
24-33
2018
Escherichia coli (P05523), Escherichia coli
Li, H.; Endutkin, A.V.; Bergonzo, C.; Campbell, A.J.; de los Santos, C.; Grollman, A.; Zharkov, D.O.; Simmerling, C.
A dynamic checkpoint in oxidative lesion discrimination by formamidopyrimidine-DNA glycosylase
Nucleic Acids Res.
44
683-694
2016
Escherichia coli (P05523), Geobacillus stearothermophilus (P84131)
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