BRENDA - Enzyme Database
show all sequences of 3.1.3.35

Deoxythymidylate phosphohydrolase from PBS2 phage-infected Bacillus subtilis

Price, A.R.; Methods Enzymol. 51, 285-290 (1978)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Bacillus subtilis
Hg2+
-
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
dTMP
-
Bacillus subtilis
0.8
-
dUMP
-
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute for Mg2+ in activation
Bacillus subtilis
Mg2+
Km: 0.06 mM
Bacillus subtilis
Ni2+
can substitute for Mg2+ in activation
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
gel filtration
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dTMP + H2O
Bacillus subtilis
functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection
thymidine + phosphate
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
infected with phage PBS2
-
Purification (Commentary)
Commentary
Organism
partial
Bacillus subtilis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
113
-
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
deoxythymidine 5'-phosphate + H2O
-
81085
Bacillus subtilis
deoxythymidine + phosphate
-
-
-
?
dGMP + H2O
-
81085
Bacillus subtilis
deoxyguanosine + phosphate
-
-
-
?
dTMP + H2O
functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection
81085
Bacillus subtilis
thymidine + phosphate
-
-
-
-
dUMP + H2O
-
81085
Bacillus subtilis
deoxyuridine + phosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.8
6.8
-
Bacillus subtilis
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
10.5
inactivated above pH 10.5 and below pH 4.5
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Bacillus subtilis
Hg2+
-
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
dTMP
-
Bacillus subtilis
0.8
-
dUMP
-
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute for Mg2+ in activation
Bacillus subtilis
Mg2+
Km: 0.06 mM
Bacillus subtilis
Ni2+
can substitute for Mg2+ in activation
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
gel filtration
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dTMP + H2O
Bacillus subtilis
functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection
thymidine + phosphate
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Bacillus subtilis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
113
-
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
deoxythymidine 5'-phosphate + H2O
-
81085
Bacillus subtilis
deoxythymidine + phosphate
-
-
-
?
dGMP + H2O
-
81085
Bacillus subtilis
deoxyguanosine + phosphate
-
-
-
?
dTMP + H2O
functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection
81085
Bacillus subtilis
thymidine + phosphate
-
-
-
-
dUMP + H2O
-
81085
Bacillus subtilis
deoxyuridine + phosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.8
6.8
-
Bacillus subtilis
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
10.5
inactivated above pH 10.5 and below pH 4.5
Bacillus subtilis
Other publictions for EC 3.1.3.35
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)
650698
Lee
Overproduction of thymidine by ...
Bacillus phage PBS2
Biotechnol. Lett.
26
265-268
2004
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
650791
He
Involvement of a substrate cyc ...
Mus musculus
Cell. Physiol. Biochem.
12
305-314
2002
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652211
Cook
The delta subunit of type 6 ph ...
Bos taurus, Bos taurus PDE6
J. Biol. Chem.
276
5248-5255
2001
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
81088
Fisher
Isozyme phenotypes of polyoma ...
Mus musculus
Cancer Res.
43
3783-3792
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
81087
Schaer
Thymidine nucleotide synthesis ...
Cricetulus griseus
Biochim. Biophys. Acta
697
221-228
1982
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
81085
Price
Deoxythymidylate phosphohydrol ...
Bacillus subtilis
Methods Enzymol.
51
285-290
1978
-
-
-
-
-
-
2
2
-
3
1
1
-
2
-
-
1
-
-
-
1
-
4
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
3
1
1
-
-
-
1
-
-
1
-
4
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
81086
Price
Deoxythymidylate phosphohydrol ...
Bacillus subtilis
J. Biol. Chem.
248
1372-1380
1973
-
-
-
-
-
-
9
2
-
1
-
-
-
3
-
-
1
-
-
-
-
1
11
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
9
-
2
-
1
-
-
-
-
-
1
-
-
-
1
11
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
81084
Vasken Aposhian
Deoxythymidylate 5-nucleotidas ...
Bacillus subtilis
J. Biol. Chem.
241
5095-5101
1966
-
-
-
-
-
-
4
3
-
2
-
-
-
3
-
-
1
-
-
-
-
-
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
3
-
2
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-