Information on EC 3.2.2.23 - DNA-formamidopyrimidine glycosylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.2.23
-
RECOMMENDED NAME
GeneOntology No.
DNA-formamidopyrimidine glycosylase
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
show the reaction diagram
mechanism
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
reaction mechanism
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
kinetic mechanism
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
catalytic mechanism
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
catalytic mechanism
Escherichia coli JM109
-
-
hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
show the reaction diagram
mechanism
Escherichia coli B834 (DE3), Escherichia coli BH20
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase
-
-
-
-
2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase
-
-
-
-
2,6-diamino-4-hydroxy-5N-methyl-formamidopyrimidine-DNA glycosylase
-
-
-
-
8-hydroxyguanine endonuclease
-
-
-
-
8-oxoguanine DNA glycosylase
-
-
-
-
8-oxoguanine-DNA glycosylase
O15527
-
deoxyribonucleate glycosidase
-
-
-
-
DNA glycohydrolase (releasing 2,6-diamino-4-hydroxy-5-(N-methyl)-formamidopyrimidine)
-
-
-
-
DNA glycosylase
-
-
endonuclease VIII-like DNA glycosylase
-
-
Fapy DNA glycosylase
-
-
Fapy-DNA glycosylase
-
-
-
-
Fapy-DNA glycosylase
A5U6T0, P9WNC3
-
Fapy-DNA glycosylase
A5U6T0, P9WNC3
-
-
formamidopyrimidineDNA glycosylase
-
-
formamidopyrimidine DNA glycosylase
Q88AH6
-
formamidopyrimidine DNA glycosylase
-
-
formamidopyrimidine DNA glycosylase
-
-
formamidopyrimidine glycosylase
O80358
-
formamidopyrimidine-DNA glycosyl hydrolase
-
-
-
-
formamidopyrimidine-DNA glycosylase
-
-
-
-
formamidopyrimidine-DNA glycosylase
-
-
formamidopyrimidine-DNA glycosylase
-
-
formamidopyrimidine-DNA glycosylase
A5U6T0, P9WNC3
-
formamidopyrimidine-DNA glycosylase
A5U6T0, P9WNC3
-
-
formamidopyrimidine-N-glycosylase
-
-
formamidopyrimidine-N-glycosylase
Escherichia coli SR108
-
-
-
FPG
-
-
-
-
FPG
Escherichia coli SR108
-
-
-
FPG
A5U6T0, P9WNC3
-
FPG
A5U6T0, P9WNC3
-
-
Fpg protein
-
-
-
-
FPG-1
O80358
-
FPG-2
O80358
-
Fpg-L
P42371
-
Mtb-Fpg1
A5U6T0, P9WNC3
-
Mtb-Fpg1
A5U6T0, P9WNC3
-
-
MutM
-
-
-
-
NEH1
Q96FI4
human homolog to MutM and Nei
NEH2
Q969S2
human homolog to MutM and Nei
NEIL1
Mus musculus C57BL/6
-
-
-
NEIL3
-
-
OGG1
O15527
-
glycosidase, deoxyribonucleate formamidopyrimidine
-
-
-
-
additional information
Q88AH6
Fpg is one of several DNA glycosylases in Arabidopsis thaliana
additional information
-
Fpg belongs to the class of DNA glycosylases/abasic site lyases
additional information
-
the enzymes belong to the Fpg family of DNA glycosylases
CAS REGISTRY NUMBER
COMMENTARY
78783-53-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AtFPG-1, enzyme exists in 2 splicing variants: AtFPG-1 and -2; AtFPG-2, enzyme exists in 2 splicing variants: AtFPG-1 and -2
SwissProt
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
isozymes FPG-1 and FPG-2, genes fpg-1 and fpg-2
SwissProt
Manually annotated by BRENDA team
gene fpg
-
-
Manually annotated by BRENDA team
expression in CHO cell
-
-
Manually annotated by BRENDA team
gene fpg
-
-
Manually annotated by BRENDA team
strain 5H11S
SwissProt
Manually annotated by BRENDA team
strain B834 (DE3) harboring PET13a-fpg plasmid
-
-
Manually annotated by BRENDA team
strain BH20 containing pFPG220
-
-
Manually annotated by BRENDA team
strain HB101 hosting pFPG60 plasmid
-
-
Manually annotated by BRENDA team
strain HB1100
-
-
Manually annotated by BRENDA team
strain JM109
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain W
-
-
Manually annotated by BRENDA team
Escherichia coli 5H11S
strain 5H11S
SwissProt
Manually annotated by BRENDA team
Escherichia coli B834 (DE3)
strain B834 (DE3) harboring PET13a-fpg plasmid
-
-
Manually annotated by BRENDA team
Escherichia coli BH20
strain BH20 containing pFPG220
-
-
Manually annotated by BRENDA team
Escherichia coli HB1100
strain HB1100
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli SR108
-
-
-
Manually annotated by BRENDA team
children with Down's syndrome
-
-
Manually annotated by BRENDA team
human nei homolog NEH1
GenBank
Manually annotated by BRENDA team
human nei homolog NEH2
UniProt
Manually annotated by BRENDA team
isoform hOGG1
-
-
Manually annotated by BRENDA team
isoform Ogg1
-
-
Manually annotated by BRENDA team
isoform Ogg1, patients with gastric cancer
-
-
Manually annotated by BRENDA team
white-collar active smokers and passive smokers at workplace
-
-
Manually annotated by BRENDA team
subspecies cremoris ML3
SwissProt
Manually annotated by BRENDA team
C57/BL6 mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57/BL6 mice
-
-
Manually annotated by BRENDA team
exposed to thinner fumes
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
csb-/- mice with Cockayne syndrome, a segmental premature aging syndrome with progressive neurological degeneration caused by mutations in CS complementation groups A, CSA, or B, CSB, genes, show increased 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine concentrations in in genomic DNA and mtDNA, and reduced repair function due to mutation of the endonuclease VIII-like DNA glycosylase NEIL1, overview
malfunction
-
mice lacking both NTH1 and NEIL1 demonstrate a marked increase in pulmonary and hepatic tumorigenesis compared to mice lacking either NTH1 or NEIL1. Specifically, the lung tumors contain a point mutation in codon 12 of the K-ras oncogene which is a GGT to GAT transition, overview
malfunction
O15527
OGG1 polymorphisms might be associated with succeptibility of humans to cancer and other diseases
malfunction
-
patients with Cockayne syndrome, a segmental premature aging syndrome with progressive neurological degeneration caused by mutations in CS complementation groups A, CSA, or B, CSB, genes, show increased 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine concentrations in in genomic DNA and mtDNA, and reduced repair function due to mutation of the endonuclease VIII-like DNA glycosylase NEIL1, overview
malfunction
-
there is significant accumulation of 2,6-diamino-4-hydroxy-5-formamidopyrimidine, (5'R)-8,5'-cyclo-2'-deoxyadenosine and (5'S)-8,5'-cyclo-2'-deoxyadenosine in liver DNA of neil1knockout mice that are not exposed to exogenous oxidative stress
malfunction
Mus musculus C57BL/6
-
mice lacking both NTH1 and NEIL1 demonstrate a marked increase in pulmonary and hepatic tumorigenesis compared to mice lacking either NTH1 or NEIL1. Specifically, the lung tumors contain a point mutation in codon 12 of the K-ras oncogene which is a GGT to GAT transition, overview
-
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
-
NEIL1 plays a role during transcription
physiological function
-
Neil3 plays a role in repairing 2,6-diamino-4-hydroxy-5-formamidopyrimidine in vivo
physiological function
O15527
OGG1 is part of an enzymatic system responsible for prevention of mutations generated by 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine
physiological function
-
the enzyme initiates the process of repair of oxidized DNA bases
physiological function
-
NEIL1 is a DNA glycosylase that is involved in the first step of base excision repair of oxidatively induced DNA damage. NEIL1 is involved in nucleotide excision repair of (5'R)-8,5'-cyclo-2'-deoxyadenosine and (5'S)-8,5'-cyclo-2'-deoxyadenosine
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
Escherichia coli SR108
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
13mer oligonucleotide duplex containing 8-oxoguanine + H2O
8-oxoguanine + oligonucleotide
show the reaction diagram
-
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
show the reaction diagram
-
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
show the reaction diagram
O15527
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
show the reaction diagram
O15527
-
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
show the reaction diagram
-
DHU is excised from DNA by a number of DNA glycosylases including Fpg and Nei, DHU is formed in DNA from cytosine under the action of OH radicals under ionizing radiation
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
show the reaction diagram
-
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
show the reaction diagram
O15527
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O
8-oxo-7,8-dihydroguanine + Cyt-DNA
show the reaction diagram
O15527
-
-
-
?
depurinated supercoiled plasmid DNA + H2O
?
show the reaction diagram
-
the degree of supercoiling of assay plasmid DNA does not affect enzyme activity
-
-
?
DNA + H2O
?
show the reaction diagram
-
substrate specificity
-
-
?
DNA + H2O
?
show the reaction diagram
-
substrate specificity
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
substrate specificity
-
-
?
DNA + H2O
?
show the reaction diagram
O80358
both AtFPG-1 and -2 cleave DNA containing apurinic sites and UV-irradiated and oxidized DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines, from oxidatively damaged DNA, DNA glycosylase/AP lyase activity, substrate recognition
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
-
-
?
DNA + H2O
?
show the reaction diagram
-
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
-
-
?
DNA + H2O
?
show the reaction diagram
-
role of Lys-155 for substrate binding and product release, AP lyase mechanism
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
excises formamidopyrimidines from damaged DNA and oxidized pyrimidines and 8-oxoguanine from oligodeoxynucleotides, role of the N-terminal Pro as its active site
-
-
?
DNA + H2O
?
show the reaction diagram
-
FpG-DNA interactions establish contacts with DNA ligands, which span no more than 9 base-pairs, structural studies of Fpg-DNA complexes
-
-
?
DNA + H2O
?
show the reaction diagram
-
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, removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
active site is located within the first 73 amino acids of the N-terminus
-
-
?
DNA + H2O
?
show the reaction diagram
-
excises purine bases with ring-opened imidazoles, associated activity that nicks DNA at apurinic/apyrimidinic sites, mechanism of cleavage involves beta elimination
-
-
?
DNA + H2O
?
show the reaction diagram
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
P42371
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
-
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
-
-
?
DNA + H2O
?
show the reaction diagram
O80358
catalyzes the initial steps in the repair of DNA containing oxidized purines
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA repair enzyme specific for the removal of purine-derived lesions from DNA damaged by free radicals and other oxidative processes
-
-
?
DNA + H2O
?
show the reaction diagram
-
plays an important role in base excision repair of oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
involved in replication-associated repair of oxidized bases
-
-
?
DNA + H2O
?
show the reaction diagram
P42371
important role in protecting DNA against oxidative free radicals and reactive oxygen-derived species
-
-
?
DNA + H2O
?
show the reaction diagram
-
biological substrates are purine oxidation products
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli JM109
-
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity, DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli B834 (DE3)
-
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions, FpG-DNA interactions establish contacts with DNA ligands, which span no more than 9 base-pairs, structural studies of Fpg-DNA complexes, enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity, bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli BH20
-
removes oxidized purines from oxidatively damaged DNA, enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity, involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli BH20
-
removes oxidized purines from oxidatively damaged DNA, enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli K12
-
substrate specificity
-
-
?
DNA containing 2'-deoxy-8-oxonebularine residues + H2O
?
show the reaction diagram
P50465
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
show the reaction diagram
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
-
similar specificity as FapyAde-DNA, better substrate than 8-hydroxyguanine-DNA
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
-
removal with similar specificity as 4,6-diamino-5-formamidopyrimidine and 8-hydroxyguanine, FapyGua
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
P50465
FapyGua
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
-
FapyGua
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
-
FapyGua
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
Q969S2, Q96FI4
FapyGua
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
show the reaction diagram
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
show the reaction diagram
P05523
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
DNA + 2,6-diamino-4-hydroxy-5-formamidopyrimidine
show the reaction diagram
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxyformamidopyrimidine residues + H2O
2,6-diamino-4-hydroxyformamidopyrimidine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
similar specificity as FapyGua-DNA, better substrate than 8-hydroxyguanine-DNA
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
-
FapyAde
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
P50465
FapyAde
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
-
FapyAde
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
-
FapyAde
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
show the reaction diagram
Q969S2, Q96FI4
FapyAde
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
show the reaction diagram
P05523
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
show the reaction diagram
-
-
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
DNA + 4,6-diamino-5-formamidopyrimidine
show the reaction diagram
Escherichia coli SR108
-
-
-
-
?
DNA containing 5,6-dihydrothymine residues + H2O
?
show the reaction diagram
-
dublex 33mer oligonucleotide, poor substrate
-
-
?
DNA containing 5,6-dihydrouracil + H2O
DNA + 5,6-dihydrouracil
show the reaction diagram
-
-
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine + H2O
?
show the reaction diagram
-
double-stranded oligonucleotides, N-glycosylase/beta,delta-elimination reaction
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine + H2O
?
show the reaction diagram
Q969S2, Q96FI4
dublex oligodeoxynucleotide containing 5-hydroxyuracil when paired with G
-
-
?
DNA containing 5-hydroxy-5-methylhydantoin residues opposite cytosine + H2O
5-hydroxy-5-methylhydantoin + DNA
show the reaction diagram
-
excellent substrate when the lesion is opposite a cytosine, poor substrate when the lesion is opposite a adenine
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
?
show the reaction diagram
-
double-stranded oligonucleotides containing 5-hydroxy-2'-deoxycytidine, N-glycosylase/beta,delta-elimination reaction
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
?
show the reaction diagram
-
dublex 33mer oligonucleotide, excision mechanism
-
-
?
DNA containing 5-hydroxycytosine residues + H2O
5-hydroxycytosine + DNA
show the reaction diagram
Escherichia coli, Escherichia coli SR108
-
-
-
-
-
DNA containing 5-hydroxyuracil residues + H2O
5-hydroxyuracil + DNA
show the reaction diagram
Escherichia coli, Escherichia coli SR108
-
-
-
-
-
DNA containing 7-deaza-2'-deoxyguanosine + H2O
7-deaza-2'-deoxyguanosine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
dublex, primary physiological substrate, DNA repair
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
-
-
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
P50465
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
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
-
removes 8-oxoguanine from oxidatively damaged DNA
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
P50465
DNA glycosylase/AP lyase activity
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
-
DNA glycosylase/AP lyase activity
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
Q969S2, Q96FI4
excises 8-oxoguanine from 31mer oligodeoxynucleotide, most active with G, followed by T, opposite the lesion, weak activity with C or A opposite
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
-
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
show the reaction diagram
-
mechanism involving protonation at O-6 of 8-oxodeoxyguanine
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
-
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
show the reaction diagram
-
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 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
Escherichia coli JM109
-
mechanism involving protonation at O-6 of 8-oxodeoxyguanine, 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-methyl-8-oxo-2'-deoxyguanosine + H2O
7-methyl-8-oxo-2'-deoxyguanosine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 8-hydroxyadenine + H2O
DNA + 8-hydroxyguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-hydroxyadenine residues + H2O
8-hydroxyadenine + DNA
show the reaction diagram
-
poor substrate
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
-
-
-
-
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
DNA glycosylase/AP lyase activity
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
34mer oligonucleotide containing a single 7,8-dihydro-8-oxoguanine residue
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
P42371
34mer oligonucleotide containing a single 7,8-dihydro-8-oxoguanine residue
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O80358
AtFPG-1, but not AtFPG-2, cleaves double-stranded oligonucleotides containing 8-oxoguanine
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
mendatory role of P-2 in 7,8-dihydro-8-oxoguanine-DNA glycosylase activity
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
7,8-dihydro-8-oxo-2-deoxyguanosine, natural substrate, substrate recognition, mechanism
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
P42371
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
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
formamidopyrimidines are preferred over 8-hydroxyguanine
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
7,8-dihydro-8-oxoguanine-DNA
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
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-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
Escherichia coli BH20
-
-
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
Escherichia coli BH20
-
DNA glycosylase/AP lyase activity, 34mer oligonucleotide containing a single 7,8-dihydro-8-oxoguanine residue
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
Escherichia coli K12
-
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, 7,8-dihydro-8-oxoguanine-DNA
-
-
?
DNA containing 8-oxo-2'-deoxyguanosine + H2O
8-oxo-2'-deoxyguanosine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxo-2'-deoxyinosine + H2O
?
show the reaction diagram
-
dublex
-
-
?
DNA containing 8-oxo-7,8-dihydroguanine residues + H2O
DNA + 8-hydroxyguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxo-7,8-dihydroguanine residues + H2O
DNA + 8-oxo-7,8-dihydroguanine
show the reaction diagram
P05523
-
-
-
?
DNA containing 8-oxo-7,8-dihydropurine + H2O
8-oxo-7,8-dihydropurine + DNA
show the reaction diagram
-
poor substrate when the lesion is opposite a cytosine
-
-
?
DNA containing 8-oxo-guanine residues + H2O
DNA + 8-oxoguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxo-guanine residues mispaired to adenine + H2O
DNA + 8-oxoguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxo-guanine residues mispaired to guanine + H2O
DNA + 8-oxoguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxo-guanine residues mispaired to thymine + H2O
DNA + 8-oxoguanine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxoguanine opposite A + H2O
8-oxoguanine + DNA
show the reaction diagram
-
poor substrate, analysis of rate constants of conformational transitions
-
-
?
DNA containing 8-oxoguanine opposite C + H2O
8-oxoguanine + DNA
show the reaction diagram
-
good substrate, analysis of rate constants of conformational transitions
-
-
?
DNA containing 8-oxoguanine opposite G + H2O
8-oxoguanine + DNA
show the reaction diagram
-
analysis of rate constants of conformational transitions
-
-
?
DNA containing 8-oxoguanine opposite T + H2O
8-oxoguanine + DNA
show the reaction diagram
-
analysis of rate constants of conformational transitions
-
-
?
DNA containing 8-oxoguanine residues + H2O
8-oxoguanine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxoguanine residues + H2O
8-oxoguanine + DNA
show the reaction diagram
-
8-oxoguanine residues opposite cytosine
-
-
?
DNA containing 8-oxoguanine residues + H2O
8-oxoguanine + DNA
show the reaction diagram
Escherichia coli SR108
-
-
-
-
?
DNA containing 8-thio-2'-deoxyguanosine + H2O
8-thio-2'-deoxyguanosine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing dihydrothymine residues + H2O
dihydrothymine + DNA
show the reaction diagram
-
-
-
-
-
DNA containing dihydrouracil + H2O
8-oxoguanine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing dihydrouracil residues + H2O
?
show the reaction diagram
Q969S2, Q96FI4
active as a DNA glycosylase/AP lyase with dihydrouracil 31mer dublex oligo substrate, similar activity with A, C or G opposite the lesion, reduced with T opposite
-
-
?
DNA containing guanidinohydantoin + H2O
guanidinohydantoin + DNA
show the reaction diagram
-
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 ring-opened N7-methylguanine + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
P42371
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dublex oligodeoxynucleotides containing Me-Fapy
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
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
show the reaction diagram
P50465
23-oligomer
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli, Escherichia coli JM109
-
amino terminal localization of the catalytic site
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
Escherichia coli BH20
-
-
-
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
Escherichia coli K12
-
dublex oligodeoxynucleotides containing Me-Fapy
-
?
DNA containing ring-opened N7-methylguanine residues + H2O
2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
show the reaction diagram
Escherichia coli HB1100
-
enzyme excises the secondary alkylation product of 7-methylguanine Fapy
-
?
oligonucleotide containing 8-oxo-2'-deoxyguanosine residue + H2O
oligonucleotide + 8-oxo-2'-deoxyguanosine
show the reaction diagram
-
-
-
-
?
oligonucleotide containing abasic site residue + H2O
oligonucleotide + abasic site
show the reaction diagram
-
-
-
-
?
oligonucleotide containing tetrahydrofuran residue + H2O
oligonucleotide + tetrahydrofuran
show the reaction diagram
-
-
-
-
?
DNA containing spiroiminodihydantoin + H2O
spiroiminodihydantoin + DNA
show the reaction diagram
-
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
-
-
?
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
?
-
Q969S2, Q96FI4
not: DNA containing 2-hydroxyadenine, 1-N6 ethenoadenine, 3-N4 ethenocytosine, hypoxanthine, xanthine
-
-
-
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 eight phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L249 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
-
-
-
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
?
-
-
treatment of cells with 4-(acetoxymethylnitrosamino)-1-(3-pyridyl)-1-butanone generates formamidopyrimidine glycosylase sensitive DNA sites with cell-type dependent differences in adduct frequency and time
-
-
-
additional information
?
-
O15527
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
-
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
?
-
-
MmuNeil3 is a bifunctional DNA glycosylase that recognizes spiroiminodihydantoin and guanidinohydantoin, as well as 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, in double-stranded substrates. Neil3 greatly reduces both the spontaneous mutation frequency and the level of 2,6-diamino-4-hydroxy-5-formamidopyrimidine in the DNA. Substrate specificity of MmuNeil3 in vivo, overview
-
-
-
additional information
?
-
-
NEIL1 is active on DNA lesions in ssDNA, particularly in the context of a single-stranded bubble in a duplex sequence
-
-
-
additional information
?
-
O15527
8-oxoguanine-DNA glycosylase, OGG1, efficiently removes mutagenic 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine when paired with cytosine in oxidatively damaged DNA. Excision of 8-oxoGua mispaired with adenine may lead to G to T transversions. Substrate specificity of wild-type and mutant enzymes, 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
?
-
-
Fpg prefers thymine glycol, 5-hydroxycytosine, 5-hydroxyuracil, 5,6-dihydrothymine and 5,6-dihydrouracil, over 7,8-dihydro-8-oxoguanine, the oxidation products of 8-oxoG namely, Gh:C, Sp1:C and Sp2:C are the best substrates for the enzyme, single-stranded DNA is also a substrate, no activity with 8-oxoguanine, Fpg substrate specificity, overview
-
-
-
additional information
?
-
Q88AH6
Fpg prefers thymine glycol, 5-hydroxycytosine, 5-hydroxyuracil, 5,6-dihydrothymine and 5,6-dihydrouracil, over 7,8-dihydro-8-oxoguanine, the oxidation products of 8-oxoG namely, Gh:C, Sp1:C and Sp2:C are the best substrates for the enzyme, single-stranded DNA is also a substrate, no activity with 8-oxoguanine, Fpg substrate specificity, overview
-
-
-
additional information
?
-
-
in duplex DNA, mouse Neil3 recognizes the oxidized purines, spiroiminodihydantoin, guanidinohydantoin, 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, but not 8-oxo-7,8-dihydroguanine. Neil3 prefers lesions in single-stranded DNA and in bubble structures. Mouse Neil3 forms a Schiff base intermediate via its N-terminal valine, in contrast to other enzyme of the family that use proline as nucleophile
-
-
-
additional information
?
-
A5U6T0, P9WNC3
Mtb-Fpg1 removes formamidopyrimidine and 5-hydroxycytosine lesions, as well as 8-oxo-7,8-dihydroguanine opposite to C, T and G. Substrates are duplex DNA substrates containing a single 8oxoG opposite of C, A, G, T, 5-hydroxycytosine (5OHC):G, 5-hydroxyuracil (5OHU):G, DHU:G, U:A or U:G base pair
-
-
-
additional information
?
-
-
formamidopyrimidine DNA glycosylase is specific for oxidized purines
-
-
-
additional information
?
-
-
the enzyme has no specificity for DNA containing 8-hydroxyguanine residues
-
-
-
additional information
?
-
-
the enzyme is a DNA glycosylase/AP lyase specific for oxidized purines such as 8-oxo-7,8-dihydropurines and imidazole-ring opened purines (2,6-diamino-4-hydroxy-5-formamidopyrimidine and formamidopyrimidine derived from adenine)
-
-
-
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
?
-
A5U6T0, P9WNC3
Mtb-Fpg1 removes formamidopyrimidine and 5-hydroxycytosine lesions, as well as 8-oxo-7,8-dihydroguanine opposite to C, T and G. Substrates are duplex DNA substrates containing a single 8oxoG opposite of C, A, G, T, 5-hydroxycytosine (5OHC):G, 5-hydroxyuracil (5OHU):G, DHU:G, U:A or U:G base pair
-
-
-
additional information
?
-
Escherichia coli B834 (DE3)
-
not: carbocyclic substrate analog of 8-oxo-7,8-dihydro-2-deoxyguanosine
-
-
-
additional information
?
-
Escherichia coli K12
-
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
?
-
Escherichia coli SR108
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,6-diamino-4-hydroxy-5-formamidopyrimidine-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
show the reaction diagram
-
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
show the reaction diagram
O15527
-
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
show the reaction diagram
-
DHU is excised from DNA by a number of DNA glycosylases including Fpg and Nei
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
show the reaction diagram
-
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O
8-oxo-7,8-dihydroguanine + Cyt-DNA
show the reaction diagram
O15527
-
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
O80358
catalyzes the initial steps in the repair of DNA containing oxidized purines
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA repair enzyme specific for the removal of purine-derived lesions from DNA damaged by free radicals and other oxidative processes
-
-
?
DNA + H2O
?
show the reaction diagram
-
plays an important role in base excision repair of oxidatively damaged DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
involved in replication-associated repair of oxidized bases
-
-
?
DNA + H2O
?
show the reaction diagram
P42371
important role in protecting DNA against oxidative free radicals and reactive oxygen-derived species
-
-
?
DNA + H2O
?
show the reaction diagram
-
biological substrates are purine oxidation products
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
P50465
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
Q969S2, Q96FI4
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli JM109
-
DNA base excision repair enzyme
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli B834 (DE3)
-
bifunctional base excision repair enzyme: DNA glycosylase/AP lyase
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli BH20
-
involved in the repair of oxidized purines generated in the genome by endogenous or exogenous oxidative stress
-
-
?
DNA + H2O
?
show the reaction diagram
Escherichia coli BH20
-
removes oxidized purines from oxidatively damaged DNA
-
-
?
DNA containing 2,6-diamino-4-hydroxyformamidopyrimidine residues + H2O
2,6-diamino-4-hydroxyformamidopyrimidine + DNA
show the reaction diagram
-
repair of the major DNA lesions 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxyformamidopyrimidine formed by reactive oxidative species
-
-
?
DNA containing 7-hydro-8-oxoguanine + H2O
7-hydro-8-oxoguanine + DNA
show the reaction diagram
-
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
show the reaction diagram
-
dublex, primary physiological substrate, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair
-
-
?
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
-
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-methylformamidopyrimidine + DNA
show the reaction diagram
-
repairs oxidative DNA damage by efficiently removing formamidopyrimidine lesions and 8-oxoguanine residues from 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
?
-
O15527
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
-
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
?
-
-
MmuNeil3 is a bifunctional DNA glycosylase that recognizes spiroiminodihydantoin and guanidinohydantoin, as well as 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, in double-stranded substrates. Neil3 greatly reduces both the spontaneous mutation frequency and the level of 2,6-diamino-4-hydroxy-5-formamidopyrimidine in the DNA. Substrate specificity of MmuNeil3 in vivo, overview
-
-
-
additional information
?
-
-
NEIL1 is active on DNA lesions in ssDNA, particularly in the context of a single-stranded bubble in a duplex sequence
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
zinc(II)- and cobalt(II)-associated enzyme, metal-binding domain
KCl
-
stimulates
KCl
-
optimum concentration: 0.1 M; stimulates
Na+
-
maximal efficiency at 100 mM NaCl
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
Zn2+
P42371
contains a single zinc finger motif near the C-terminus; contains one zinc per enzyme molecule
Zn2+
-
contains a four cystein-zinc finger motif
Zn2+
-
possesses a zinc finger
Zn2+
-
contains a single zinc finger motif near the C-terminus
Zn2+
-
contains one zinc per enzyme molecule; possesses a zinc finger
KH2PO4
-
pH 7.4, stimulates, optimum concentration: 0.05 M
additional information
O80358
no zinc finger
additional information
Q969S2, Q96FI4
no zinc finger
additional information
-
NEIL1 is not affected by Mg2+, Mn2+, and Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-Nitroso-2,4,6-triaminopyrimidine
-
product inhibition
Al3+
-
-
Cd2+
-
preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA
Co2+
-
-
Cu2+
-
preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA
d(pA)10-d(pT)10
-
dublex, nonspecific oligonucleotide
-
d(pA)16-d(pT)16
-
dublex, nonspecific oligonucleotide
-
DNA containing 2-deoxyribonolactone residues
-
suicide inhibitor for formamidopyrimidine-DNA glycosylase
-
DNA containing 5-hydroxy-5-methylhydantoin residues
-
suicide inhibitor for formamidopyrimidine-DNA glycosylase
-
Fe2+
-
-
Ni2+
-
0.001 mM, inhibition
Ni2+
-
-
nonspecific ds 8-23mer oligonucleotide
-
competitive inhibitors
-
tetrahydrofuran-containing DNA dublex
-
-
-
Zn2+
-
-
Formamidopyrimidine
-
product inhibition
additional information
-
not inhibited by 1.2 mM 8-oxo-7,8-dihydro-2-deoxyguanosine
-
additional information
-
differing inhibitory effects of metal ions in potassiumphosphate buffer and Tris-HCl buffer, mechanism of NEIL1 inhibition by heavy metal salts, e.g. involving sequential elimination of phosphate groups from the 3'- and 5'-side of the formed AP site, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
complementation groups B genes
-
CSB stimulates incision activity of NEIL1, and CSB stimulates the NEIL1-mediated AP lyase activity 3fold
-
complementation groups B genes
-
CSB stimulates incision activity of NEIL1
-
additional information
O15527
the human AP endonuclease APEX1 can stimulate wild-type OGG1 activity by increasing its turnover rate, but very little stimulation of 8-oxoGua removal in the presence of APEX1 occurs with phosphomimetic mutants, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000181
13mer oligonucleotide duplex containing 8-oxoguanine
-
15C
-
0.0000222
13mer oligonucleotide duplex containing 8-oxoguanine
-
17.5C
-
0.0000296
13mer oligonucleotide duplex containing 8-oxoguanine
-
20C
-
0.0000369
13mer oligonucleotide duplex containing 8-oxoguanine
-
22.5C
-
0.0000466
13mer oligonucleotide duplex containing 8-oxoguanine
-
25C
-
0.00015
5,6-dihydrouracil-DNA
-
NEIL1
-
0.0000034
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S326C; pH 7.4-7.5, wild-type enzyme
-
0.0000057
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S231E
-
0.0000061
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant D322N
-
0.0000074
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S280E
-
0.0000075
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S326E
-
0.0000086
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant A288V
-
0.0000092
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S232E
-
0.00001
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S231E/S232E
-
0.0000009
DNA
P50465
pH 7.5, 20C, 24-oligomer DNA containing apurinic/apyrimidinic sites, lyase activity, K155A mutant Fpg
0.000019
DNA
P50465
pH 7.5, 20C, 24-oligomer DNA containing AP sites, lyase activity, wild-type Fpg
0.0046
DNA
-
pH 7.5, 25C, DNA containing an apurinic/apyrimidinic site
0.00178
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37C, K57R mutant Fpg, from DNA gamma-irradiated under NO2
-
0.00187
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37C, 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, 37C, wild-type Fpg
-
0.00422
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
-
pH 7.4, 37C, 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, 37C, 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, 37C, K57G mutant Fpg
-
0.00079 - 0.0009
DNA containing 4,6-diamino-5-formamidopyrimidine residues
-
pH 7.4, 37C, K57R mutant Fpg
-
0.00107 - 0.00129
DNA containing 4,6-diamino-5-formamidopyrimidine residues
-
pH 7.4, 37C, wild-type Fpg
-
0.00045
DNA containing 5,6-dihydrothymine residues
-
pH 7.5, 37C
-
0.00061
DNA containing 5,6-dihydrouracil
-
mutant K217A
0.00068
DNA containing 5,6-dihydrouracil
-
wild-type
0.0007
DNA containing 5,6-dihydrouracil
-
mutant H89A; mutant R108A
0.00465
DNA containing 5,6-dihydrouracil
-
mutant R109A
0.00957
DNA containing 5,6-dihydrouracil
-
mutant H89A/R109A
0.0047
DNA containing 5-hydroxycytosine residues
-
pH 7.5, 37C
-
0.000083
DNA containing 7-deaza-2'-deoxyguanosine
-
-
0.000126
DNA containing 7-deaza-2'-deoxyguanosine
-
-
0.0000069
DNA containing 7-hydro-8-oxoguanine residues
P50465
pH 7.5, 37C, 24-oligomer, wild-type Fpg
-
0.0000075
DNA containing 7-hydro-8-oxoguanine residues
P50465
pH 7.5, 37C, 24-oligomer, K155A mutant Fpg
-
0.002
DNA containing 7-hydro-8-oxoguanine residues
-
pH 7.5, 25C
-
0.000053
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
-
-
0.000137
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
-
-
0.000004
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37C, 34-oligomer, wild-type and K57R mutant Fpg
-
0.000008
DNA containing 8-hydroxyguanine residues
-
pH 7.5, 20C, dublex DNA containing a single 8-oxoguanine residue positioned opposite dC
-
0.000008
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37C, 34-oligomer, K57G mutant Fpg
-
0.000013
DNA containing 8-hydroxyguanine residues
-
pH 7.5, 37C
-
0.00093 - 0.00155
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37C, K57R mutant Fpg
-
0.00109
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37C, wild-type Fpg, from DNA treated with H2O2/Fe(III)-EDTA/asc
-
0.00126
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37C, K57G mutant Fpg
-
0.00311
DNA containing 8-hydroxyguanine residues
-
pH 7.4, 37C, wild-type Fpg, from DNA gamma-irradiated under NO2
-
0.000012
DNA containing 8-oxo-2'-deoxyguanosine
-
-
0.001
DNA containing 8-oxo-guanine residues
-
wild-type
-
0.0015
DNA containing 8-oxo-guanine residues
-
mutant R108A
-
0.0041
DNA containing 8-oxo-guanine residues
-
mutant H89A; mutant K217T
-
0.227
DNA containing 8-oxo-guanine residues
-
mutant R109A
-
0.44
DNA containing 8-oxo-guanine residues
-
mutant H89A/R109A
-
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
-
0.000151
DNA containing 8-thio-2'-deoxyguanosine
-
-
0.000225
DNA containing 8-thio-2'-deoxyguanosine
-
-
0.000009 - 0.000011
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37C, wild-type, K57G and K57R mutant Fpg
-
0.000023
DNA containing ring-opened N7-methylguanine residues
P50465
pH 7.5, 37C, 23-oligomer, wild-type Fpg
-
0.000029
DNA containing ring-opened N7-methylguanine residues
P50465
pH 7.5, 37C, 23-oligomer, K155A mutant Fpg
-
0.000038
DNA containing ring-opened N7-methylguanine residues
-
pH 7.5, 37C
-
0.000041
DNA containing ring-opened N7-methylguanine residues
-
pH 7.5, 20C, dublex DNA containing a single Me-Fapy residue positioned opposite dC
-
additional information
additional information
-
kinetic parameters of duplex oligonucleotides and mismatched duplexes
-
additional information
additional information
-
Km for DNA substrate is affected by the base opposite the lesion
-
additional information
additional information
-
Km values for excision of purine lesions from DNA treated with various free radical-generating systems
-
additional information
additional information
-
thermodynamic characterization of Fpg binding to lesion-containing 13mer DNA dublexes, binding affinity
-
additional information
additional information
-
steady state kinetics
-
additional information
additional information
-
kinetics, detailed overview
-
additional information
additional information
Q88AH6
Fpg single-turnover kinetics, overview
-
additional information
additional information
-
Fpg single-turnover kinetics, overview
-
additional information
additional information
-
transient kinetics of Fpg
-
additional information
additional information
-
steady-state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
13mer oligonucleotide duplex containing 8-oxoguanine
-
15C
-
0.0106
13mer oligonucleotide duplex containing 8-oxoguanine
-
17.5C
-
0.0148
13mer oligonucleotide duplex containing 8-oxoguanine
-
20C
-
0.0202
13mer oligonucleotide duplex containing 8-oxoguanine
-
22.5C
-
0.0273
13mer oligonucleotide duplex containing 8-oxoguanine
-
25C
-
0.02
5,6-dihydrouracil-DNA
-
NEIL1
-
0.00037
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S326C
-
0.00047
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant D322N
-
0.00048
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S280E
-
0.0005
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, wild-type enzyme
-
0.00053
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S326E
-
0.00065
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S232E
-
0.00068
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S231E/S232E
-
0.0007
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant S231E
-
0.00092
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
O15527
pH 7.4-7.5, mutant A288V
-
0.05
DNA
-
pH 7.5, 25C, DNA containing an apurininc/apyrimidinic site
0.0568
DNA
P50465
pH 7.5, 20C, 24-oligomer DNA containing AP sites, lyase activity, wild-type Fpg
0.0883
DNA
P50465
pH 7.5, 20C, 24-oligomer DNA containing AP sites, lyase activity, K155A mutant Fpg
0.004
DNA containing 5,6-dihydrouracil
-
mutant H89A/R109A
0.0053
DNA containing 5,6-dihydrouracil
-
mutant R108A; mutant R109A
0.0093
DNA containing 5,6-dihydrouracil
-
mutant K217A
0.011
DNA containing 5,6-dihydrouracil
-
wild-type
0.015
DNA containing 5,6-dihydrouracil
-
mutant H89A
0.00078
DNA containing 7-deaza-2'-deoxyguanosine
-
-
0.053
DNA containing 7-deaza-2'-deoxyguanosine
-
-
0.000383
DNA containing 7-hydro-8-oxoguanine residues
P50465
pH 7.5, 37C, 24-oligomer, K155A mutant Fpg
-
0.0185
DNA containing 7-hydro-8-oxoguanine residues
P50465
pH 7.5, 37C, 24-oligomer, wild-type Fpg
-
0.025
DNA containing 7-hydro-8-oxoguanine residues
-
pH 7.5, 25C
-
0.00025
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
-
-
0.00051
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
-
-
0.000167
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37C, 34-oligomer, K57G mutant Fpg
-
0.00717
DNA containing 8-hydroxyguanine residues
-
pH 7.8, 37C, 34-oligomer, wild-type Fpg
-
0.03
DNA containing 8-hydroxyguanine residues
-
pH 7.5, 37C
-
0.00167
DNA containing 8-hyroxyguanine
-
pH 7.8, 37C, 34-oligomer, K57R mutant Fpg
-
0.043
DNA containing 8-oxo-2'-deoxyguanosine
-
-
0.066
DNA containing 8-oxo-2'-deoxyguanosine
-
-
0.0003
DNA containing 8-oxo-guanine residues
-
mutant R108A
-
0.0035
DNA containing 8-oxo-guanine residues
-
mutant H89A/R109A
-
0.004
DNA containing 8-oxo-guanine residues
-
mutant K217T
-
0.005
DNA containing 8-oxo-guanine residues
-
wild-type
-
0.0059
DNA containing 8-oxo-guanine residues
-
mutant R109A
-
0.0067
DNA containing 8-oxo-guanine residues
-
mutant H89A
-
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
-
0.00045
DNA containing 8-thio-2'-deoxyguanosine
-
-
0.0012
DNA containing ring-opened N7-methylguanine residues
P50465
pH 7.5, 37C, 23-oligomer, K155A mutant Fpg
-
0.002
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37C, K57G and K57R mutant Fpg
-
0.00383
DNA containing ring-opened N7-methylguanine residues
P50465
pH 7.5, 37C, 23-oligomer, wild-type Fpg
-
0.00833
DNA containing ring-opened N7-methylguanine residues
-
pH 7.8, 37C, wild-type Fpg
-
0.085
DNA containing ring-opened N7-methylguanine residues
-
pH 7.5, 37C
-
additional information
additional information
-
turnover of duplex oligonucleotides and mismatched duplexes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0067
d(pA)10-d(pT)10
-
pH 7.5, 25C
-
0.001
d(pA)16-d(pT)16
-
pH 7.5, 25C
-
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
Cd2+
-
-
0.4
Cu2+
-
-
0.016
Zn2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0146
-
pH 7.6, 37C, enzyme from overexpressing strain HB101
0.0423
-
pH 7.6, 37C, Fapy-DNA glycosylase activity
0.054
P50465
polymeric DNA containing ring-opened N7-methylguanine residues as substrate, wild-type Fpg
0.5
-
pH 7.8, 37C, apurinic/apyrimidinic-nicking activity
additional information
-
-
additional information
P42371
-
additional information
-
-
additional information
-
molecular modeling and molecular dynamics simulation to interprete substrate discrimination in the active site
additional information
O15527
substrate specificity of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
assay at
7
Q88AH6
assay at
7
-
assay at
7.2 - 8
-
-
7.4 - 7.5
O15527
assay at
7.4
Q969S2, Q96FI4
assay at
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
assay at, 13mer substrates
20
-
assay at, 23mer substrates
22
Q88AH6
assay at room temperature
22
-
assay at room temperature
25
-
assay at
37
P50465
assay at
37
Q969S2, Q96FI4
assay at; assay at
37
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q969S2, Q96FI4
moderate expression of NEH1
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Q969S2, Q96FI4
low expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
highest expression of NEH1 in liver, pancreas and thymus
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Q969S2, Q96FI4
primary human diploid fibroblasts, S phase-specific expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
moderate expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
highest expression of NEH1 in liver, pancreas and thymus
Manually annotated by BRENDA team
Q969S2, Q96FI4
moderate expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
moderate expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
low expression of NEH1
Manually annotated by BRENDA team
Q969S2, Q96FI4
highest expression of NEH1 in liver, pancreas and thymus
Manually annotated by BRENDA team
additional information
A5U6T0, P9WNC3
molecular strain typing, and enzyme expression level, overview
Manually annotated by BRENDA team
additional information
A5U6T0, P9WNC3
molecular strain typing, and enzyme expression levels in strain H37Rv and other isolates, overview
Manually annotated by BRENDA team
additional information
-
molecular strain typing, and enzyme expression levels in strain H37Rv and other isolates, overview, molecular strain typing, and enzyme expression level, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Q969S2, Q96FI4
NEH1 is not localized in mitochondria
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Lactococcus lactis subsp. cremoris (strain SK11)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
-
gel filtration
646937
30000
P42371
active form
646942
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 31000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
Q969S2, Q96FI4
x * 36800, NEH2, calculated from the amino acid sequence
?
Q969S2, Q96FI4
x * 43582, recombinant NEH1, calculated from the amino acid sequence
?
-
x * 34800, calculated from the amino acid sequence
?
O80358
x * 32400, AtFPG-2, calculated from the amino acid sequence, x * 44800, AtFPG-1, calculated from the amino acid sequence
?
-
x * 34400, SDS-PAGE
?
O80358
x * 46000, AtFPG-1, SDS-PAGE, x * 34000, AtFPG-2, SDS-PAGE
?
-
x * 30200, calculated from the amino acid sequence
?
-
x * 31950, Mtb-Fpg1, sequence calculation, x * 32000, recombinant Mtb-Fpg1, SDS-PAGE
?
-
x * 30290, calculated from amino acid sequence
?
Escherichia coli JM109
-
x * 34400, SDS-PAGE
-
?
-
x * 31950, Mtb-Fpg1, sequence calculation, x * 32000, recombinant Mtb-Fpg1, SDS-PAGE
-
?
Escherichia coli BH20, Escherichia coli HB1100
-
x * 31000, SDS-PAGE
-
?
Escherichia coli HB1100
-
x * 30200, calculated from the amino acid sequence
-
monomer
P42371
1 * 30000, SDS-PAGE
monomer
P50465
1 * 35000, SDS-PAGE
monomer
-
1 * 30200, globular monomer
monomer
P42371
1 * 31300, calculated from the amino acid sequence
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 eight phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L249 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
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
Q88AH6
AthFpg is missing the canonical zinc finger, three-dimensional structure and primary amino acid sequence in conserved structural motifs, overview
additional information
-
CalFpg is missing the canonical zinc finger, three-dimensional structure and primary amino acid sequence in conserved structural motifs, overview
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
additional information
O15527
three-dimensional structure of OGG1, PDB ID 1EBM, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
O15527
phosphorylation of OGG1 can affect its biological functions at several levels, including the intrinsic activity and intracellular localization
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
-
structure of enzyme covalently complexed to DNA
-
structures of zinc- and cobalt-associated enzyme
-
8-oxoguanine is bound via E77 in syn conformation. In mutant E77S, which reflects the sequence of the Escherichia coli enzyme, 8-oxoguanine is preferentially bound in the anti conformation
P84131
molecular dynamics simulations based on 1R2Y crystallographic data of the mutant E3Q/DNA complex. Binding of 8-oxoguanine in syn conformation is about 2.7 kcal/mol lower in energy than anti conformation
-
molecular dynamics study based on X-ray structure of enzyme bound to 8-oxoguanine-containing DNA. Presence of the damaged base influences the dynamics of the whole enzyme. Loop location is dependent on the presence and on the conformation of 8-oxoguanine in its binding site
-
crystal structure of enzyme bound to a 1,3-propanediol abasic site analogue-containing DNA
-
molecular dynamics study based on X-ray structure of enzyme bound to an abasic site analog-containing DNA
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
free protein undergoes irreversible thermal unfolding with a Tm of about 65C
646951
additional information
-
purified enzyme is very sensitive to extreme temperature fluctuations
646937
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 -20C or -80C is subsequently thawed for assaying
-
rapid loss of activity when a conventional pressure cell is used to concentrate enzyme
-
unstable in low ionic strength solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, buffered 0.5 M KCl, 1 week, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant AtFPG-1, expressed in Escherichia coli BL21(DE3); recombinant AtFPG-2, expressed in Escherichia coli BL21(DE3)
O80358
63.6fold, from overexpressing strain HB101
-
copurified with apurinic/apyrimidinic-nicking activity
-
DE52 resin column chromatography and HPLC-Shodex carboxymethyl cellulose column chromatography
-
K57R, K155A mutant Fpg; wild-type and K57G, P2G, P2E mutant Fpg
-
two-step procedure
-
wild-type and K155A mutant Fpg, expressed in Escherichia coli BLR(DE3)
P50465
wild-type and K57G, K57R mutant Fpg
-
wild-type and K57G, P2G, P2E mutant Fpg
-
wild-type, P2G, P2E and P2T mutant Fpg
-
recombinant NEH1, expressed in Escherichia coli BL21(DE3)
Q969S2, Q96FI4
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
O15527
recombinant enzyme, overexpressed in Escherichia coli BH410
P42371
recombinant Mtb-Fpg1 to homogeneity
A5U6T0, P9WNC3
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene fpg, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
Q88AH6
gene fpg, expression in Escherichia coli, expression increases the frequency of spontaneous reversions in the presence of plant FPG variant, quantitative overview
O80358
isolation of 2 cDNA clones: alternative splicing products AtFPG-1 and -2 of a single gene with different C-terminal sequences, amino acid sequences, expression of both proteins in Escherichia coli BL21(DE3)
O80358
gene fpg, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
-
Fpg gene is cloned, encodes a 273 amino acids protein
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in human bladder cell
-
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
-
expression of K155A mutant and wild-type Fpg in Escherichia coli BL21(DE3) and BLR(DE3)
P50465
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-)
-
genotyping, overview. Expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
O15527
NEH1 is cloned, sequenced and expressed in Escherichia coli BL21(DE3), chromosomal location: 15q25; NEH2, chromosomal location: 4q35
Q969S2, Q96FI4
expressed in Escherichia coli strain BH540
-
fpg-L gene is cloned, sequenced and overexpressed in Escherichia coli BH410, expression in Escherichia coli fpg and mutY mutants suppresses their spontaneous GC-TA mutator phenotype
P42371
expression of C-terminally His-tagged wild-type NEIL3 in Escherichia coli, and expression of the C-terminally His-tagged glycosylase domain of Neil3, MmuNeil3DELTA324, in an Escherichia coli triple mutant lacking Fpg, Nei, and MutY glycosylase activities, the recombinant MmuNeil3 greatly reduced both the spontaneous mutation frequency and the level of FapyG in the DNA
-
gene Rv2924c encoding Mtb-Fpg1, DNA and amino acid sequence determination and analysis, relationship between tandem repeat length and Mtb-fpg1 expression levels, quantitative expression analysis, overview
A5U6T0, P9WNC3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
H89A
-
selective diminition of the rate of excision of 8-oxoguanine
H89A/R109A
-
about 10fold increase in KM-value
K155A
-
effect of mutation on specificity, mutant with very low activity, kinetic study
K155A
P50465
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
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
K217T
-
selective reduction of the ability to excise 8-oxoguanine from DNA
K57A
-
mutant with about 15% of wild-type activity in both N-glycosylase and AP lyase activity
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
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
-
effect of mutation on specificity, inactive mutant, kinetic study
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
P2T
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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
R108A
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R108 is a major determinant of opposite-base specificity
R109A
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binding of enzyme to damaged DNA is almost abolished
K155A
Escherichia coli BH20
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mutant with reduced 8-oxoguanine-DNA but unchanged Fapy-DNA glycosylase activity
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K57G
Escherichia coli BH20
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study of the effect of the mutation on the structure dynamics, mutant with decreased 8-hydroxyguanine-DNA glycosylase activity, 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
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K57R
Escherichia coli BH20
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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
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P2E
Escherichia coli BH20
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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
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E3Q
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crystallization data
E77S
P84131
in wild-type, 8-oxoguanine is bound via E77 in syn conformation. In mutant E77S, which reflects the sequence of the Escherichia coli enzyme, 8-oxoguanine is preferentially bound in the anti conformation
A288V
O15527
naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1, activity, substrate specificity and kinetics compared to the wild-type enzyme, overview
S1245C
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naturally occuring polymorphism. No correlation between mutation and gastric cancer
S231E
O15527
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S231E/S232E
O15527
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S232E
O15527
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S280E
O15527
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S326C
O15527
naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1. The mutant efficiently excises 8-oxoGua from oligodeoxynucleotides and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from gamma-irradiated DNA, but excises 8-oxoG rather inefficiently from gamma-irradiated DNA
K57R
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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
additional information
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mutant Fpg protein with NH2-terminal modifications
additional information
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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
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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
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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
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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
P2G
Escherichia coli BH20
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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
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additional information
Escherichia coli JM109
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mutant Fpg protein with NH2-terminal modifications
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D322N
O15527
naturally occuring polymorphism, the mutant is 2.3fold more specific for the correct opposite base than the wild-type enzyme, activity, substrate specificity and kinetics compared to the wild-type enzyme
additional information
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study on the polymorphism 23A to G in the DNA repair gene XPA. Presence of the A allele is associated with higher levels of DNA damage as well as with higher activity of the OGG1 8-oxoguanidine DNA glycosylase. In individuals with the A allele, OGG1 repair activity also increases with age
additional information
O15527
the gene shows several polymorphisms in vivo
S326E
O15527
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
additional information
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the content of 2,6-diamino-4-hydroxy-5-formamidopyrimidine derived guanine is increased in some but not all tissues of Neil1-/- mice
additional information
Mus musculus C57BL/6
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the content of 2,6-diamino-4-hydroxy-5-formamidopyrimidine derived guanine is increased in some but not all tissues of Neil1-/- mice
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additional information
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gene disruption mutants exhibits an enhanced mutator phenotype and susceptibility to hydrogen peroxide as well as a remarkable increase in accumulation of A to G (or T to C) mutations. Exposure of the mutant to sub-lethal level of hydrogen peroxide results in a major shift toward C to G (or G to C) mutations
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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
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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
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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
analysis
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comparison of human Ogg1, Escherichia coli Fpg and endonuclease III for the ability to modify the sensitivity of the comet assay. 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
analysis
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DNA repair kinetics can be investigated with the comet assay and differences between cell types can be observed
medicine
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cells from children with Down's syndrome do not display an effective DNA repair after treatment with 10 mM hydrogen peroxide. No difference in the sensitivity to DNA-damaging agents and the efficacy of DNA repair due to age and gender in children with Down's syndrome is observed
medicine
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melatonin can have a protective effect against oxidative DNA damage by chemical inactivation of a DNA-damaging agent as well as by stimulating DNA repair, but key factors such as DNA-formaidopyrimidine glycosylase, endonuclease III are not affected by melatonin
medicine
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no correlation between the S1245C polymorphism of the OGG! Gene and gastric cancer. In contrast, there is a strong correlation between gastric cancer occurrence, impaired DNA repair in human lymphocytes, and the G135C polymorphism of the RAD51 gene
medicine
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significant amounts of 85% of enzyme-sensitive DNA sites are found in smokers, and considerably high but not significant amounts in passive non- and ex-smokers, 51 and 37%, respectively
medicine
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study on the polymorphism 23A to G in the DNA repair gene XPA. Presence of the A allele is associated with higher levels of DNA damage as well as with higher activity of the OGG1 8-oxoguanidine DNA glycosylase. In individuals with the A allele, OGG1 repair activity also increases with age
medicine
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treatment of cells with 4-(acetoxymethylnitrosamino)-1-(3-pyridyl)-1-butanone generates formamidopyrimidine glycosylase sensitive DNA sites with cell-type dependent differences in adduct frequency and time
medicine
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lymphocytes of rats exposed to thinner fumes exhibits a significant increase in enzyme-sensitive DNA sites compared with control. The most abundant base oxidation product is 8-oxoguanine, which is the main substrate of enzyme