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 hide
3.2.2.23
-
RECOMMENDED NAME
GeneOntology No.
DNA-formamidopyrimidine glycosylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
78783-53-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene fpg
-
-
Manually annotated by BRENDA team
strain 5H11S
SwissProt
Manually annotated by BRENDA team
Escherichia coli B834 (DE3)
strain B834 (DE3) harboring PET13a-fpg plasmid
-
-
Manually annotated by BRENDA team
strain BH20 containing pFPG220
-
-
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
-
-
-
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
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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
-
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
show the reaction diagram
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
-
-
-
?
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
DNA containing 2'-deoxy-8-oxonebularine residues + H2O
?
show the reaction diagram
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
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
DNA + 4,6-diamino-5-formamidopyrimidine
show the reaction diagram
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
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
5-hydroxycytosine + DNA
show the reaction diagram
DNA containing 5-hydroxycytosine residues + H2O
?
show the reaction diagram
DNA containing 5-hydroxyuracil residues + H2O
5-hydroxyuracil + DNA
show the reaction diagram
DNA containing 7,8-dihydro-8-oxoguanine residues + H2O
DNA + 7,8-dihydro-8-oxoguanine
show the reaction diagram
-
-
-
-
?
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
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
show the reaction diagram
DNA containing 7-methyl-7-deazaguanine residues + H2O
7-methyl-7-deazaguanine + DNA
show the reaction diagram
-
-
-
-
?
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-oxo-2'-deoxyguanosine + H2O
8-oxo-2'-deoxyguanosine + DNA
show the reaction diagram
DNA containing 8-oxo-2'-deoxyguanosine residues + H2O
DNA + 8-oxo-2'-deoxyguanosine
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
-
-
-
?
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
DNA + 8-oxoguanine
show the reaction diagram
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
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 formamidopyrimidine-guanine residues + H2O
formamidopyrimidine-guanine + DNA
show the reaction diagram
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 methylated formamidopyrimidine-guanine residues + H2O
methylated formamidopyrimidine-guanine + DNA
show the reaction diagram
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 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
-
-
?
DNA containing tetrahydrofuran residues + H2O
tetrahydrofuran + DNA
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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
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
DNA containing 8-hydroxyguanine residues + H2O
8-hydroxyguanine + DNA
show the reaction diagram
DNA containing 8-oxo-2'-deoxyguanosine residues + H2O
DNA + 8-oxo-2'-deoxyguanosine
show the reaction diagram
-
-
-
-
?
DNA containing 8-oxoguanine residues + H2O
DNA + 8-oxoguanine
show the reaction diagram
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
zinc(II)- and cobalt(II)-associated enzyme, metal-binding domain
KH2PO4
-
pH 7.4, stimulates, optimum concentration: 0.05 M
Na+
-
maximal efficiency at 100 mM NaCl
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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+
-
-
Formamidopyrimidine
-
product inhibition
nonspecific ds 8-23mer oligonucleotide
-
competitive inhibitors
-
tetrahydrofuran-containing DNA dublex
-
-
-
Zn2+
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
complementation groups B genes
additional information
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 hide
LITERATURE
IMAGE
0.0000181 - 0.0000466
13mer oligonucleotide duplex containing 8-oxoguanine
0.00015
5,6-dihydrouracil-DNA
-
NEIL1
-
0.0000034 - 0.00001
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
0.0000009 - 0.0046
DNA
0.00178 - 0.00487
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues
0.00078 - 0.00129
DNA containing 4,6-diamino-5-formamidopyrimidine residues
0.00045
DNA containing 5,6-dihydrothymine residues
-
pH 7.5, 37C
-
0.00061 - 0.00957
DNA containing 5,6-dihydrouracil
0.0047
DNA containing 5-hydroxycytosine residues
-
pH 7.5, 37C
-
0.000083 - 0.000126
DNA containing 7-deaza-2'-deoxyguanosine
0.0000069 - 0.002
DNA containing 7-hydro-8-oxoguanine residues
0.000053 - 0.000137
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
0.000004 - 0.00311
DNA containing 8-hydroxyguanine residues
0.000012
DNA containing 8-oxo-2'-deoxyguanosine
0.001 - 0.44
DNA containing 8-oxo-guanine residues
0.022 - 0.023
DNA containing 8-oxo-guanine residues mispaired to adenine
0.0001 - 0.0051
DNA containing 8-oxo-guanine residues mispaired to guanine
0.00019 - 0.0042
DNA containing 8-oxo-guanine residues mispaired to thymine
0.000151 - 0.000225
DNA containing 8-thio-2'-deoxyguanosine
0.000009 - 0.000041
DNA containing ring-opened N7-methylguanine residues
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.0273
13mer oligonucleotide duplex containing 8-oxoguanine
0.02
5,6-dihydrouracil-DNA
Homo sapiens
-
NEIL1
-
0.00037 - 0.00092
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
0.05 - 0.0883
DNA
0.004 - 0.015
DNA containing 5,6-dihydrouracil
0.00078 - 0.053
DNA containing 7-deaza-2'-deoxyguanosine
0.000383 - 0.025
DNA containing 7-hydro-8-oxoguanine residues
0.00025 - 0.00051
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine
0.000167 - 0.03
DNA containing 8-hydroxyguanine residues
0.00167
DNA containing 8-hyroxyguanine
Escherichia coli
-
pH 7.8, 37C, 34-oligomer, K57R mutant Fpg
-
0.043 - 0.066
DNA containing 8-oxo-2'-deoxyguanosine
0.0003 - 0.0067
DNA containing 8-oxo-guanine residues
0.000075 - 0.00011
DNA containing 8-oxo-guanine residues mispaired to adenine
0.00038 - 0.0035
DNA containing 8-oxo-guanine residues mispaired to guanine
0.0003 - 0.0047
DNA containing 8-oxo-guanine residues mispaired to thymine
0.00045
DNA containing 8-thio-2'-deoxyguanosine
0.0012 - 0.085
DNA containing ring-opened N7-methylguanine residues
additional information
additional information
Escherichia coli
-
turnover of duplex oligonucleotides and mismatched duplexes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.007
Cd2+
Homo sapiens
-
-
0.4
Cu2+
Homo sapiens
-
-
0.016
Zn2+
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0146
-
pH 7.6, 37C, enzyme from overexpressing strain HB101
0.0423
-
pH 7.6, 37C, Fapy-DNA glycosylase activity
0.054
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.2 - 8
-
-
7.4 - 7.5
assay at
7.6
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
assay at, 13mer substrates
20
-
assay at, 23mer substrates
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression of NEH1
Manually annotated by BRENDA team
primary human diploid fibroblasts, S phase-specific expression of NEH1
Manually annotated by BRENDA team
moderate expression of NEH1
Manually annotated by BRENDA team
highest expression of NEH1 in liver, pancreas and thymus
Manually annotated by BRENDA team
moderate expression of NEH1
Manually annotated by BRENDA team
moderate expression of NEH1
Manually annotated by BRENDA team
low expression of NEH1
Manually annotated by BRENDA team
highest expression of NEH1 in liver, pancreas and thymus
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Lactococcus lactis subsp. cremoris (strain SK11)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation of OGG1 can affect its biological functions at several levels, including the intrinsic activity and intracellular localization
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (v/v) PEG 2000 MME, 100 mM KBr, and 100 mM sodium acetate pH 5.0
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
-
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 hide
LITERATURE
65
-
free protein undergoes irreversible thermal unfolding with a Tm of about 65C
additional information
-
purified enzyme is very sensitive to extreme temperature fluctuations
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
15N-labeled formamidopyrimidine DNA glycosylase is as active as unlabeled enzyme
-
50% glycerol destabilizes during storage, concentration of above 10% cause a 60% reduction in activity
-
complete loss of activity if the enzyme stored at -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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, buffered 0.5 M KCl, 1 week, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
63.6fold, from overexpressing strain HB101
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copurified with apurinic/apyrimidinic-nicking activity
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DE52 resin column chromatography and HPLC-Shodex carboxymethyl cellulose column chromatography
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HiTrap nickel sulfate-charged column chromatography and HiTrap SP column chromatography
K57R, K155A mutant Fpg; wild-type and K57G, P2G, P2E mutant Fpg
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recombinant AtFPG-1, expressed in Escherichia coli BL21(DE3); recombinant AtFPG-2, expressed in Escherichia coli BL21(DE3)
recombinant enzyme, overexpressed in Escherichia coli BH410
recombinant Mtb-Fpg1 to homogeneity
recombinant NEH1, expressed in Escherichia coli BL21(DE3)
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
two-step procedure
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wild-type and K155A mutant Fpg, expressed in Escherichia coli BLR(DE3)
wild-type and K57G, K57R mutant Fpg
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wild-type and K57G, P2G, P2E mutant Fpg
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wild-type, P2G, P2E and P2T mutant Fpg
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli Rosetta (DE3) pLysS cells
expressed in Escherichia coli strain BH540
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expressed in HEK-293 cells
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expressed NCI-H727 non small cell lung carcinoma cells
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expression in Escherichia coli
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expression in human bladder cell
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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
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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
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expression of K155A mutant and wild-type Fpg in Escherichia coli BL21(DE3) and BLR(DE3)
Fpg gene is cloned, encodes a 273 amino acids protein
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fpg structural gene is cloned and sequenced, overexpression in Escherichia coli HB101
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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
gene fpg, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
gene fpg, expression in Escherichia coli, expression increases the frequency of spontaneous reversions in the presence of plant FPG variant, quantitative overview
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
genotyping, overview. Expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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)
NEH1 is cloned, sequenced and expressed in Escherichia coli BL21(DE3), chromosomal location: 15q25; NEH2, chromosomal location: 4q35
P2E, P2T and P2G mutant Fpg are cloned and expressed in Escherichia coli BH20(fpg-)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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inactive. Mutant binds DNA duplexes containing spiroiminodihydantoin or guanidinohydantoin about 1000fold more tightly over corresponding duplexes containing 8-oxoguanine
F110A
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the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps
F110W
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the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps
F111A
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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
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
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
-
R108 is a major determinant of opposite-base specificity
R109A
-
binding of enzyme to damaged DNA is almost abolished
K155A
-
mutant with reduced 8-oxoguanine-DNA but unchanged Fapy-DNA glycosylase activity
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K57G
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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; study of the effect of the mutation on the structure dynamics, mutant with decreased 8-hydroxyguanine-DNA glycosylase activity
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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
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P2E
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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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P2G
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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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E3Q
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crystallization data
E77S
-
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
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
D322N
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
S1245C
-
naturally occuring polymorphism. No correlation between mutation and gastric cancer
S231E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S231E/S232E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S232E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S280E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S326C
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
S326E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
Show AA Sequence (8168 entries)
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