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 ACCESSION NO.
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
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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; 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
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
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
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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
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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
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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
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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
-
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase
-
-
-
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2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase
-
-
-
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2,6-diamino-4-hydroxy-5N-methyl-formamidopyrimidine-DNA glycosylase
-
-
-
-
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)
-
-
-
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DNA glycosylase
-
-
endonuclease VIII-like DNA glycosylase
-
-
Fapy DNA glycosylase
-
-
Fapy-DNA glycosylase
-
-
-
-
Fapy-DNA glycosylase
A5U6T0, P64150
-
formamidopyrimidineDNA glycosylase
-
-
formamidopyrimidine DNA glycosylase
Q88AH6
-
formamidopyrimidine DNA glycosylase
-
-
formamidopyrimidine DNA glycosylase
-
-
formamidopyrimidine glycosylase
Q9SBB4
-
formamidopyrimidine-DNA glycosyl hydrolase
-
-
-
-
formamidopyrimidine-DNA glycosylase
-
-
-
-
formamidopyrimidine-DNA glycosylase
-
-
formamidopyrimidine-DNA glycosylase
-
-
formamidopyrimidine-DNA glycosylase
A5U6T0, P64150
-
formamidopyrimidine-N-glycosylase
-
-
formamidopyrimidine-N-glycosylase
Escherichia coli SR108
-
-
-
FPG
-
-
-
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FPG
Escherichia coli SR108
-
-
-
FPG
A5U6T0, P64150
-
Fpg protein
-
-
-
-
FPG-1
Q9SBB4
-
FPG-2
Q9SBB4
-
Fpg-L
P42371
-
Mtb-Fpg1
A5U6T0, P64150
-
MutM
-
-
-
-
NEH1
Q96FI4
human homolog to MutM and Nei
NEH2
Q969S2
human homolog to MutM and Nei
NEIL3
-
-
OGG1
O15527
-
glycosidase, deoxyribonucleate formamidopyrimidine
-
-
-
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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
SEQUENCE CODE
SEQUENCE DB
SOURCE
AtFPG-1, enzyme exists in 2 splicing variants: AtFPG-1 and -2
Q9SBB4
SwissProt
Manually annotated by BRENDA team
AtFPG-2, enzyme exists in 2 splicing variants: AtFPG-1 and -2
O80359
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
Q9SBB4
SwissProt
Manually annotated by BRENDA team
gene fpg
-
-
Manually annotated by BRENDA team
expression in CHO cell
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-
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
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-
Manually annotated by BRENDA team
strain BH20 containing pFPG220
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-
Manually annotated by BRENDA team
strain HB101 hosting pFPG60 plasmid
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-
Manually annotated by BRENDA team
strain HB1100
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-
Manually annotated by BRENDA team
strain JM109
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-
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
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-
Manually annotated by BRENDA team
Escherichia coli BH20
strain BH20 containing pFPG220
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-
Manually annotated by BRENDA team
Escherichia coli HB1100
strain HB1100
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
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-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
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-
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
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-
Manually annotated by BRENDA team
isoform Ogg1
-
-
Manually annotated by BRENDA team
isoform Ogg1, patients with gastric cancer
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-
Manually annotated by BRENDA team
white-collar active smokers and passive smokers at workplace
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-
Manually annotated by BRENDA team
subspecies cremoris ML3
SwissProt
Manually annotated by BRENDA team
C57/BL6 mice
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-
Manually annotated by BRENDA team
exposed to thinner fumes
-
-
Manually annotated by BRENDA team
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0067
-
d(pA)10-d(pT)10
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pH 7.5, 25C
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0.001
-
d(pA)16-d(pT)16
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pH 7.5, 25C
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additional information
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additional information
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with increase in dublex length of nonspecific ds 8-23mer oligonucleotides, Ki values decrease from 0.05 mM to 0.0007 mM
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PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Lactococcus lactis subsp. cremoris (strain SK11)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
15N-labeled formamidopyrimidine DNA glycosylase is as active as unlabeled enzyme
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50% glycerol destabilizes during storage, concentration of above 10% cause a 60% reduction in activity
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complete loss of activity if the enzyme stored at -20C or -80C is subsequently thawed for assaying
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rapid loss of activity when a conventional pressure cell is used to concentrate enzyme
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unstable in low ionic strength solutions
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, buffered 0.5 M KCl, 1 week, stable
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