BRENDA - Enzyme Database

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
EC Number
General Stability
Organism
3.2.2.17
resistant to EDTA
Micrococcus luteus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.99.18
4-chloromercuribenzoate
complete inhibition at 1 mM
Bacillus subtilis
4.2.99.18
EDTA
96% inhibition at 20 mM
Bacillus subtilis
4.2.99.18
NaCl
complete inhibition at 1 M, 40% inhibition at 0.5 M
Bacillus subtilis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.2.17
0.000015
-
DNA
thymine labeled DNA
Micrococcus luteus
3.2.2.17
0.00028
-
DNA
cytosine labeled DNA
Micrococcus luteus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.2.2.17
17500
-
SDS-PAGE
Micrococcus luteus
3.2.2.17
18000
-
-
Micrococcus luteus
4.2.99.18
26000
-
4 * 26000, SDS-PAGE
Bacillus subtilis
4.2.99.18
105000
-
glycerol gradient centrifugation
Bacillus subtilis
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.2.2.17
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
?
-
-
-
4.2.99.18
DNA
Bacillus subtilis
-
fragments of DNA
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.2.2.17
Micrococcus luteus
-
-
-
4.2.99.18
Bacillus subtilis
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
3.2.2.17
-
Micrococcus luteus
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.99.18
additional information
-
-
Bacillus subtilis
Storage Stability
EC Number
Storage Stability
Organism
3.2.2.17
stable on ice for 8 months with no loss in activity
Micrococcus luteus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.2.2.17
DNA phiX174 RFI + H2O
irradiated with increasing doses of UV light
586960
Micrococcus luteus
thymine + ?
-
-
-
?
3.2.2.17
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
?
-
-
-
-
3.2.2.17
oligonucleotides + H2O
-
586960
Micrococcus luteus
dCMP + dTMP
-
586960
Micrococcus luteus
?
4.2.99.18
DNA
-
586960
Bacillus subtilis
fragments of DNA
-
-
-
?
4.2.99.18
DNA
hydrolyzes phosphodiester bond near heat-induced apruinic sites in double or single strand DNA
586960
Bacillus subtilis
fragments of DNA
-
586960
Bacillus subtilis
?
4.2.99.18
additional information
no substrate: alkylated sites
586960
Bacillus subtilis
?
-
-
-
-
4.2.99.18
additional information
no substrate: native DNA
586960
Bacillus subtilis
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
3.2.2.17
monomer
1 * 17500-18000, single polypeptide chain
Micrococcus luteus
4.2.99.18
tetramer
4 * 26000, SDS-PAGE
Bacillus subtilis
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.2.2.17
45
55
thermal inactivation of both endonuclease and glycosylase activity
Micrococcus luteus
General Stability (protein specific)
EC Number
General Stability
Organism
3.2.2.17
resistant to EDTA
Micrococcus luteus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.99.18
4-chloromercuribenzoate
complete inhibition at 1 mM
Bacillus subtilis
4.2.99.18
EDTA
96% inhibition at 20 mM
Bacillus subtilis
4.2.99.18
NaCl
complete inhibition at 1 M, 40% inhibition at 0.5 M
Bacillus subtilis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.2.17
0.000015
-
DNA
thymine labeled DNA
Micrococcus luteus
3.2.2.17
0.00028
-
DNA
cytosine labeled DNA
Micrococcus luteus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.2.2.17
17500
-
SDS-PAGE
Micrococcus luteus
3.2.2.17
18000
-
-
Micrococcus luteus
4.2.99.18
26000
-
4 * 26000, SDS-PAGE
Bacillus subtilis
4.2.99.18
105000
-
glycerol gradient centrifugation
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.2.2.17
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
?
-
-
-
4.2.99.18
DNA
Bacillus subtilis
-
fragments of DNA
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.2.2.17
-
Micrococcus luteus
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.99.18
additional information
-
-
Bacillus subtilis
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
3.2.2.17
stable on ice for 8 months with no loss in activity
Micrococcus luteus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.2.2.17
DNA phiX174 RFI + H2O
irradiated with increasing doses of UV light
586960
Micrococcus luteus
thymine + ?
-
-
-
?
3.2.2.17
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
?
-
-
-
-
3.2.2.17
oligonucleotides + H2O
-
586960
Micrococcus luteus
dCMP + dTMP
-
586960
Micrococcus luteus
?
4.2.99.18
DNA
-
586960
Bacillus subtilis
fragments of DNA
-
-
-
?
4.2.99.18
DNA
hydrolyzes phosphodiester bond near heat-induced apruinic sites in double or single strand DNA
586960
Bacillus subtilis
fragments of DNA
-
586960
Bacillus subtilis
?
4.2.99.18
additional information
no substrate: alkylated sites
586960
Bacillus subtilis
?
-
-
-
-
4.2.99.18
additional information
no substrate: native DNA
586960
Bacillus subtilis
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.2.2.17
monomer
1 * 17500-18000, single polypeptide chain
Micrococcus luteus
4.2.99.18
tetramer
4 * 26000, SDS-PAGE
Bacillus subtilis
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.2.2.17
45
55
thermal inactivation of both endonuclease and glycosylase activity
Micrococcus luteus