BRENDA - Enzyme Database
show all sequences of 3.2.2.17

Enzymatic repair of pyrimidine dimer-containing DNA. A 5' dimer DNA glycosylase: 3'-apyrimidinic endonuclease mechanism from Micrococcus luteus

Grafstrom, R.H.; Park, L.; Grossman, L.; J. Biol. Chem. 257, 13465-13474 (1982)

Data extracted from this reference:

General Stability
General Stability
Organism
resistant to EDTA
Micrococcus luteus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000015
-
DNA
thymine labeled DNA
Micrococcus luteus
0.00028
-
DNA
cytosine labeled DNA
Micrococcus luteus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17500
-
SDS-PAGE
Micrococcus luteus
18000
-
-
Micrococcus luteus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Micrococcus luteus
only nicking of UV-irradiated DNA, creating phospho diester bond breaks 5' with respect to pyrimidine dimers, protein containing the glycosylase activity also contains the apyrimidinic endonuclease activity, multifunctional enzyme, 2 distinct domains in a single enzyme molecule possess both pyrimidine dimer-DNA glycosylase, and AP endonuclease activity, first the glycosylase cleaves glycosylic bond of one of the pyrimidine residues of a dimer to yield an AP site, then AP endonuclease hydrolyzes the phospho diester bond near the AP site, prefers duplex DNA to single-stranded
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Micrococcus luteus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Micrococcus luteus
Storage Stability
Storage Stability
Organism
stable on ice for 8 months with no loss in activity
Micrococcus luteus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DNA phiX174 RFI + H2O
irradiated with increasing doses of UV light
586960
Micrococcus luteus
thymine + ?
-
-
-
?
additional information
only nicking of UV-irradiated DNA, creating phospho diester bond breaks 5' with respect to pyrimidine dimers, protein containing the glycosylase activity also contains the apyrimidinic endonuclease activity, multifunctional enzyme, 2 distinct domains in a single enzyme molecule possess both pyrimidine dimer-DNA glycosylase, and AP endonuclease activity, first the glycosylase cleaves glycosylic bond of one of the pyrimidine residues of a dimer to yield an AP site, then AP endonuclease hydrolyzes the phospho diester bond near the AP site, prefers duplex DNA to single-stranded
586960
Micrococcus luteus
?
-
-
-
-
oligonucleotides + H2O
-
586960
Micrococcus luteus
dCMP + dTMP
-
586960
Micrococcus luteus
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 17500-18000, single polypeptide chain
Micrococcus luteus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
55
thermal inactivation of both endonuclease and glycosylase activity
Micrococcus luteus
General Stability (protein specific)
General Stability
Organism
resistant to EDTA
Micrococcus luteus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000015
-
DNA
thymine labeled DNA
Micrococcus luteus
0.00028
-
DNA
cytosine labeled DNA
Micrococcus luteus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17500
-
SDS-PAGE
Micrococcus luteus
18000
-
-
Micrococcus luteus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Micrococcus luteus
only nicking of UV-irradiated DNA, creating phospho diester bond breaks 5' with respect to pyrimidine dimers, protein containing the glycosylase activity also contains the apyrimidinic endonuclease activity, multifunctional enzyme, 2 distinct domains in a single enzyme molecule possess both pyrimidine dimer-DNA glycosylase, and AP endonuclease activity, first the glycosylase cleaves glycosylic bond of one of the pyrimidine residues of a dimer to yield an AP site, then AP endonuclease hydrolyzes the phospho diester bond near the AP site, prefers duplex DNA to single-stranded
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Micrococcus luteus
Storage Stability (protein specific)
Storage Stability
Organism
stable on ice for 8 months with no loss in activity
Micrococcus luteus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DNA phiX174 RFI + H2O
irradiated with increasing doses of UV light
586960
Micrococcus luteus
thymine + ?
-
-
-
?
additional information
only nicking of UV-irradiated DNA, creating phospho diester bond breaks 5' with respect to pyrimidine dimers, protein containing the glycosylase activity also contains the apyrimidinic endonuclease activity, multifunctional enzyme, 2 distinct domains in a single enzyme molecule possess both pyrimidine dimer-DNA glycosylase, and AP endonuclease activity, first the glycosylase cleaves glycosylic bond of one of the pyrimidine residues of a dimer to yield an AP site, then AP endonuclease hydrolyzes the phospho diester bond near the AP site, prefers duplex DNA to single-stranded
586960
Micrococcus luteus
?
-
-
-
-
oligonucleotides + H2O
-
586960
Micrococcus luteus
dCMP + dTMP
-
586960
Micrococcus luteus
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 17500-18000, single polypeptide chain
Micrococcus luteus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
55
thermal inactivation of both endonuclease and glycosylase activity
Micrococcus luteus
Other publictions for EC 3.2.2.17
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732684
Dodson
Carbinolamine formation and de ...
Escherichia virus T4
PLoS ONE
7
e31377
2012
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1
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710256
Hacker
Enhancement of DNA repair usin ...
Escherichia virus T4
Pigment Cell Melanoma Res.
23
121-128
2010
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1
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1
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4
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1
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679415
Emanuel
A review of DNA repair and pos ...
Escherichia virus T4
Dermatol. Online J.
13(3)
10
2007
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1
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682279
Jiang
-
Application of the comet assay ...
Escherichia virus T4
Physiol. Plant.
129
652-657
2007
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1
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1
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678169
Walker
Uncoupling of nucleotide flipp ...
Escherichia virus T4
Biochemistry
45
14192-14200
2006
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2
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1
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681339
Kang
-
High-level expression of T4 en ...
Escherichia virus T4
J. Microbiol. Biotechnol.
16
1583-1590
2006
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1
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1
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681394
Golan
Structure of T4 pyrimidine dim ...
Escherichia virus T4
J. Mol. Biol.
362
241-258
2006
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1
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1
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682057
Chelico
Quantification of ultraviolet- ...
Escherichia virus T4
Mycologia
97
621-627
2006
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1
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1
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682201
Bennett
Characterization of the aldehy ...
Escherichia virus T4
Nucleosides Nucleotides Nucleic Acids
25
823-842
2006
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2
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656231
Meador
Role of His-16 in turnover of ...
Escherichia coli, Escherichia virus T4
J. Biol. Chem.
279
3348-3353
2004
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1
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12
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3
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1
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12
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1
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656903
Jaruga
Chlorella virus pyrimidine dim ...
Paramecium bursaria Chlorella virus 1
Photochem. Photobiol.
75
85-91
2002
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1
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2
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5
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1
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654599
McCullough
The reaction mechanism of DNA ...
Escherichia coli
Biochemistry
40
561-568
2001
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1
2
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171811
Garvish
Active-site determination of a ...
Paramecium bursaria Chlorella virus 1
J. Mol. Biol.
295
479-488
2000
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1
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3
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171812
Sun
Intron conservation in a UV-sp ...
Escherichia virus T4, Paramecium bursaria Chlorella virus 1
J. Mol. Evol.
50
82-92
2000
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1
1
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2
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656843
Vasquez
Purification and characterizat ...
Lysinibacillus sphaericus
Mutat. Res.
459
307-316
2000
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1
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1
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171810
Garvish
The catalytic mechanism of a p ...
Escherichia virus T4, Paramecium bursaria Chlorella virus 1
J. Biol. Chem.
274
9786-9794
1999
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6
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171809
McCullough
Characterization of a novel ci ...
Escherichia virus T4, Micrococcus luteus, Paramecium bursaria Chlorella virus 1
J. Biol. Chem.
273
13136-13142
1998
1
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1
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1
4
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4
3
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7
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1
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6
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1
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1
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1
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4
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3
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2
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1
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6
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1
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1
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171808
Nyaga
Role of specific amino acid re ...
Escherichia virus T4
Biochemistry
36
4080-4088
1997
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1
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4
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171813
Green
Structure/function analysis of ...
Escherichia virus T4
Nucleic Acids Res.
21
727-732
1993
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1
1
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171807
Doi
Role of the basic amino acid c ...
Escherichia virus T4
Proc. Natl. Acad. Sci. USA
89
9420-9424
1992
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1
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170703
Ishida
In vitro and in vivo activitie ...
Escherichia virus T4
Biochemistry
29
3817-3821
1990
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1
1
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2
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5
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171803
Bailly
Bacteriophage-T4 and Micrococc ...
Escherichia virus T4, Micrococcus luteus
Biochem. J.
259
751-759
1989
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170697
Recinos
Site-directed mutagenesis of t ...
Escherichia virus T4
Biochemistry
27
1832-1838
1988
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170698
Stump
Site-directed mutagenesis of t ...
Escherichia virus T4
Biochemistry
27
1839-1843
1988
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171805
Duker
Inhibition of enzymic incision ...
Escherichia virus T4
Biochemistry
24
408-412
1985
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170694
Nakabeppu
Purification and characterizat ...
Escherichia virus T4
J. Biol. Chem.
257
2556-2562
1982
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1
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171798
Radany
Demonstration of pyrimidine di ...
Escherichia virus T4
J. Virol.
41
88-96
1982
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586960
Grafstrom
Enzymatic repair of pyrimidine ...
Micrococcus luteus
J. Biol. Chem.
257
13465-13474
1982
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170706
Nakabeppu
Physical association of pyrimi ...
Escherichia virus T4
Proc. Natl. Acad. Sci. USA
78
2742-2746
1981
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171795
Warner
-
Evidence that the UV endonucle ...
Escherichia virus T4, Micrococcus luteus
J. Virol.
10
204-210
1981
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171796
McMillan
denV gene of bacteriophage T4 ...
Escherichia virus T4, Escherichia virus T4 T4denV+
J. Virol.
40
211-223
1981
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171793
Radany
-
A pyrimidine dimer-DNA glycosy ...
Escherichia virus T4
Nature
286
183-185
1980
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171794
Haseltine
Cleavage of pyrimidine dimers ...
Micrococcus luteus
Nature
285
634-641
1980
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171801
Gordon
Comparison of the cleavage of ...
Micrococcus luteus
J. Biol. Chem.
255
12047-12050
1980
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171802
Seawell
DenV gene of bacteriophage T4 ...
Escherichia virus T4, Escherichia virus T4 T4denV1
J. Virol.
35
790-797
1980
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