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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
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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
-
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
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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
N168D
0.2% of wild-type activity
N168Q
9.5% of wild-type activity
P2T
-
mutant with 10% of wild-type 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA glycosylase activity and barely detectable 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no cleavage of DNA containing AP sites
Q234R
mutant retains activity
Q234R/R244E
mutant retains activity
R108A
-
R108 is a major determinant of opposite-base specificity
R108K
1.9% of wild-type activity
R108L
0.3% of wild-type activity
R108Q
0.3% of wild-type activity
R109A
-
binding of enzyme to damaged DNA is almost abolished
R244E
mutant retains activity
R258A
0.4% of wild-type activity
R258K
0.3% of wild-type activity
R258Q
6.2% of wild-type activity
R54E/E131R
loss of activity
S208A
mutation has no effect, in both wild-type and S208 A residue Tyr170 quickly reorients to form an alternative set of hydrogen bonds
Y170F
mutation decreases Fpg binding but does not fully inactivate the protein
K155A
-
mutant with reduced 8-oxoguanine-DNA but unchanged Fapy-DNA glycosylase activity
-
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
-
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
-
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
-
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
K155A
-
effect of mutation on specificity, mutant with very low activity, kinetic study
K155A
mutant with 50fold decreased activity with 7-hydro-8-oxoguanine-DNA as substrate, only 3-4fold decreased activity with 7-methylformamidopyrimidine-DNA, increased AP lyase activity
K155A
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mutant with reduced 8-oxoguanine-DNA but unchanged Fapy-DNA glycosylase activity
K155A
-
mutant enzyme with decreased N-glycosylase and increased AP lyase activity, it dissociates prematurely from the covalent enzyme-DNA complex leading to a higher turnover number for DNA containing an AP site
K57G
-
study of the effect of the mutation on the structure dynamics, mutant with decreased 8-hydroxyguanine-DNA glycosylase activity
K57G
-
mutant has dramatically reduced 7,8-dihydro-8-oxoguanine-DNA glycosylase activity and is poorly effective in formation of Schiff base complex with 8-oxoG/C, little effect on 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine-DNA glycosylase activity, no effect on DNA nicking activity at abasic sites
K57G
-
effect of mutation on specificity, mutant removes FapyAde and FapyGua with reduced activity compared to wild-type Fpg, kinetic study
K57R
-
effect of mutation on specificity, mutant removes FapyAde and FapyGua with reduced activity compared to wild-type Fpg, kinetic study
K57R
-
slight effect of mutation on 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no effect on 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine-DNA glycosylase activity and on DNA nicking activity at abasic sites
P2E
-
study of the effect of the mutation on the structure dynamics, mutation causes complete loss of DNA glycosylase/beta-lyase activity and induces a conformational change leading to a more rigid globular structure than wild-type, K57G and P2G Fpg
P2E
-
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
K57G
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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
-
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
additional information
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mutant Fpg protein with NH2-terminal modifications
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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
the gene shows several polymorphisms in vivo
additional information
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the gene shows several polymorphisms in vivo
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
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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