Information on EC 3.2.2.B5 - 8-oxoguanine DNA glycosylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.2.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
8-oxoguanine DNA glycosylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
DNA containing 8-oxoguanine + H2O = DNA with an abasic site + 8-oxoguanine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
DNA glycohydrolase [8-oxoguanine releasing]
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
show the reaction diagram
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
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
catalytic activity is inhibited in buffer more than 100 mM NaCl
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2
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calculated from sequence
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.5
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pH 7.3: about 50% of maximal activity, pH 9.5: about 45% of maximal ativity, glycosylase/lyase activity is very similar to that of the glycosylase activity alone
7.5 - 10
pH 7.5: about 50% of maximal activity, pH 10.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
since the Tm-value of the DNA substrates (39-mer) of is 74C, the activity above 60C is not convincible. The actual optimum temperature of the enzyme might be higher than 60C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 50
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the enzyme is 6fold more active at 50C than at 37C, glycosylase/lyase activity is very similarto that of the glycosylase activity alone
40 - 80
40C: about 60% of maximal activity, 80C: about 70% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
1 * 22000, SDS-PAGE
22639
1 * 22639, calculated from sequenec
23000
gel filtration
23124
1 * 23124, mass spectrophotometry
29467
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x * 29467, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 22000, SDS-PAGE; 1 * 22639, calculated from sequenec; 1 * 23124, mass spectrophotometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion at 12C. A structural comparison with 8-oxoguanine DNA glycosylase 1 and archaeal GO glycosylase suggests that the C-terminal lysine of 8-oxoguanine DNA glycosylase 2 may play a key role in discriminating between guanine and 8-oxoguanine
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hanging-drop, vapor-diffusion method at 12C. A single crystal of the mutant enzyme K129Q in complex with a 15-mer duplex DNA oligonucleotide containing 8-oxoG paired with C is used to collect a 2.7 A data
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crystal structure of the enzyme and that of its complex with 8-oxo-guanosine at 1.0 and 1.7 A resolution, respectively, are grown by sitting drops method
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hanging-drop vapor diffusion at 12C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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3 h, activity is decreased by one-third
78
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Tm-value for mutant enzyme W69F
84
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Tm-value for mutant enzyme D172Q
86
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Tm-value for mutant enzyme Q31S
87
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Tm-value for mutant enzyme Q31E/D218S; Tm-value for mutant enzyme W222A
88
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Tm-value for mutant enzyme W222F
additional information
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
overproduced in Escherichia coli as a maltose binding protein(MBP)-Afogg fusion protein
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D166N
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mutant enzyme shows wild-type activity
D172Q
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binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair; no detectable glycosylase activity
K147Q
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activity of mutant enzyme is severely attenuated
Q31E/D218S
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almost no glycosylase activity
Q31S
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significantly reduced glycosylase activity
W222A
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almost no glycosylase activity
W222F
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mutant is similarly active as wild type on 8-oxoguanine/C substrates
W69F
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mutant is similarly active as wild type on 8-oxoguanine/C substrates
D172N
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inactive mutant enzyme
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