BRENDA - Enzyme Database
show all sequences of 3.5.4.12

Deoxycytidylate deaminase. Evidence for a new enzyme in cells infected by the virus of Herpes simplex

Rolton, H.A.; Keir, H.M.; Biochem. J. 143, 403-409 (1974)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dCTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
Cricetinae
dCTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
Herpes simplex virus
Herpes antiserum
activation of host-cell enzyme
Cricetinae
additional information
no activation by KCl up to 0.3 M
Cricetinae
additional information
no activation by KCl up to 0.3 M
Herpes simplex virus
pre-immune serum
activation of host-cell enzyme, twice as effective as Herpes antiserum
Cricetinae
General Stability
General Stability
Organism
dCTP and Mg2+ stabilize
Cricetinae
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
Herpes simplex virus
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
Cricetinae
Inhibitors
Inhibitors
Commentary
Organism
Structure
dTTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to inhibition by dTTP than enzyme from non-infected cells
Cricetinae
dTTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to inhibition by dTTP than enzyme from non-infected cells
Herpes simplex virus
Herpes antiserum
inhibition of Herpes infected-cell enzyme
Herpes simplex virus
additional information
no inhibition by KCl up to 0.3 M
Cricetinae
additional information
no inhibition by KCl up to 0.3 M
Herpes simplex virus
pre-immune serum
inhibition of Herpes infected-cell enzyme
Herpes simplex virus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.32
-
dCMP
in the presence of dCTP and presence of 2 mM Mg2+
Cricetinae
0.32
-
dCMP
in the presence of dCTP and presence of 2 mM Mg2+
Herpes simplex virus
0.91
-
dCMP
in the presence of dCTP and absence of 2 mM Mg2+
Cricetinae
0.91
-
dCMP
in the presence of dCTP and absence of 2 mM Mg2+
Herpes simplex virus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for activation by dCTP and for inhibition by dTTP; required for complete activation by dCTP
Cricetinae
Mg2+
required for activation by dCTP and for inhibition by dTTP; required for complete activation by dCTP
Herpes simplex virus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Herpes simplex virus
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
-
?
dCMP + H2O
Cricetinae
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cricetinae
-
BHK-21/C13 cells, baby-hamster, enzyme from non-infected cells and cells infected by Herpes simplex
-
Herpes simplex virus
-
host baby-hamster, BHK-21/C13 cells; induced by
-
Purification (Commentary)
Commentary
Organism
BHK-21/C13 cells , enzyme from non-infected cells and cells infected by Herpes simplex
Cricetinae
host baby-hamster, BHK-21/C13 cells
Herpes simplex virus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
BHK-21 cell
baby-hamster kidney
Cricetinae
-
kidney
BHK-21/C13 cells, baby-hamster kidney cells
Cricetinae
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dCMP + H2O
the dCMP concentration at half-maximum velocity is lower by enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster than by enzyme from non-infected cells
289007
Herpes simplex virus
dUMP + NH3
-
289007
Herpes simplex virus
?
dCMP + H2O
the dCMP concentration at half-maximum velocity is lower by enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster than by enzyme from non-infected cells
289007
Cricetinae
dUMP + NH3
-
289007
Cricetinae
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289007
Herpes simplex virus
dUMP + NH3
-
-
-
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289007
Cricetinae
dUMP + NH3
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Cricetinae
37
-
assay at
Herpes simplex virus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilizes against heat inactivation. Host-cell enzyme is more sensitive to heating than Herpes virus infected enzyme
Cricetinae
additional information
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilizes against heat inactivation. Host-cell enzyme is more sensitive to heating than Herpes virus infected enzyme
Herpes simplex virus
37
-
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to heating at 37°C than enzyme from non-infected cells. In the presence of 0.125 mM dCTP and 2 mM Mg2+, 100% stable, 20 min at 37°C
Cricetinae
37
-
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to heating at 37°C than enzyme from non-infected cells. In the presence of 0.125 mM dCTP and 2 mM Mg2+, 100% stable, 20 min at 37°C
Herpes simplex virus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
enzyme from host-cell and Herpes virus-induced enzyme have a similar pH-optimum
Cricetinae
additional information
-
enzyme from host-cell and Herpes virus-induced enzyme have a similar pH-optimum
Herpes simplex virus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dCTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
Cricetinae
dCTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
Herpes simplex virus
Herpes antiserum
activation of host-cell enzyme
Cricetinae
additional information
no activation by KCl up to 0.3 M
Cricetinae
additional information
no activation by KCl up to 0.3 M
Herpes simplex virus
pre-immune serum
activation of host-cell enzyme, twice as effective as Herpes antiserum
Cricetinae
General Stability (protein specific)
General Stability
Organism
dCTP and Mg2+ stabilize
Cricetinae
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
Herpes simplex virus
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
Cricetinae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dTTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to inhibition by dTTP than enzyme from non-infected cells
Cricetinae
dTTP
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to inhibition by dTTP than enzyme from non-infected cells
Herpes simplex virus
Herpes antiserum
inhibition of Herpes infected-cell enzyme
Herpes simplex virus
additional information
no inhibition by KCl up to 0.3 M
Cricetinae
additional information
no inhibition by KCl up to 0.3 M
Herpes simplex virus
pre-immune serum
inhibition of Herpes infected-cell enzyme
Herpes simplex virus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.32
-
dCMP
in the presence of dCTP and presence of 2 mM Mg2+
Cricetinae
0.32
-
dCMP
in the presence of dCTP and presence of 2 mM Mg2+
Herpes simplex virus
0.91
-
dCMP
in the presence of dCTP and absence of 2 mM Mg2+
Cricetinae
0.91
-
dCMP
in the presence of dCTP and absence of 2 mM Mg2+
Herpes simplex virus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for activation by dCTP and for inhibition by dTTP; required for complete activation by dCTP
Cricetinae
Mg2+
required for activation by dCTP and for inhibition by dTTP; required for complete activation by dCTP
Herpes simplex virus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Herpes simplex virus
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
-
?
dCMP + H2O
Cricetinae
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
BHK-21/C13 cells , enzyme from non-infected cells and cells infected by Herpes simplex
Cricetinae
host baby-hamster, BHK-21/C13 cells
Herpes simplex virus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
BHK-21 cell
baby-hamster kidney
Cricetinae
-
kidney
BHK-21/C13 cells, baby-hamster kidney cells
Cricetinae
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dCMP + H2O
the dCMP concentration at half-maximum velocity is lower by enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster than by enzyme from non-infected cells
289007
Herpes simplex virus
dUMP + NH3
-
289007
Herpes simplex virus
?
dCMP + H2O
the dCMP concentration at half-maximum velocity is lower by enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster than by enzyme from non-infected cells
289007
Cricetinae
dUMP + NH3
-
289007
Cricetinae
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289007
Herpes simplex virus
dUMP + NH3
-
-
-
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289007
Cricetinae
dUMP + NH3
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Cricetinae
37
-
assay at
Herpes simplex virus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilizes against heat inactivation. Host-cell enzyme is more sensitive to heating than Herpes virus infected enzyme
Cricetinae
additional information
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilizes against heat inactivation. Host-cell enzyme is more sensitive to heating than Herpes virus infected enzyme
Herpes simplex virus
37
-
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to heating at 37°C than enzyme from non-infected cells. In the presence of 0.125 mM dCTP and 2 mM Mg2+, 100% stable, 20 min at 37°C
Cricetinae
37
-
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to heating at 37°C than enzyme from non-infected cells. In the presence of 0.125 mM dCTP and 2 mM Mg2+, 100% stable, 20 min at 37°C
Herpes simplex virus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
enzyme from host-cell and Herpes virus-induced enzyme have a similar pH-optimum
Cricetinae
additional information
-
enzyme from host-cell and Herpes virus-induced enzyme have a similar pH-optimum
Herpes simplex virus
Other publictions for EC 3.5.4.12
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)
734322
Marx
The first crystal structure of ...
Cyanophage S-TIM5
J. Biol. Chem.
290
682-690
2015
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1
1
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734401
Xu
STRIPE2 encodes a putative dCM ...
Oryza sativa
J. Genet. Genomics
41
539-548
2014
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1
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712083
Jansen
Deoxyuridine analog nucleotide ...
Homo sapiens
Fundam. Clin. Pharmacol.
25
172-185
2011
1
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8
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1
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7
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1
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711628
Li
DNA mismatch repair (MMR)-depe ...
Homo sapiens
Br. J. Pharmacol.
158
679-692
2009
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688405
Hou
Crystal structures of Streptoc ...
Streptococcus mutans
J. Mol. Biol.
377
220-231
2008
1
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5
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686248
Liskay
Involvement of deoxycytidylate ...
Saccharomyces cerevisiae
Curr. Biol.
17
R755-R757
2007
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688732
Zhang
Chloroviruses encode a bifunct ...
Paramecium bursaria Chlorella virus 1
J. Virol.
81
7662-7671
2007
1
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1
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3
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5
1
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1
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1
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2
2
1
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667587
Almog
Three-dimensional structure of ...
Escherichia virus T4
Biochemistry
43
13715-13723
2004
1
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669680
Gribaudo
Human cytomegalovirus requires ...
Homo sapiens
J. Gen. Virol.
84
1437-1441
2003
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670328
Liou
Assessment of the effect of ph ...
Homo sapiens
Mol. Pharmacol.
63
105-110
2003
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10
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667541
Cha
Modifications of deoxycytidine ...
Rattus norvegicus
Biochem. Pharmacol.
63
717-723
2002
1
-
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-
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1
4
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1
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1
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3
1
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1
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1
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4
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1
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668584
Jost
5-Methyldeoxycytidine monophos ...
Homo sapiens
FEBS Lett.
519
128-134
2002
1
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1
1
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1
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3
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289015
Keefe
A T4-phage deoxycytidylate dea ...
Enterobacteria phage T2, Enterobacteria phage T6, Escherichia virus T4
J. Biol. Chem.
275
12598-12602
2000
7
-
1
-
3
4
4
5
-
4
9
2
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4
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1
3
1
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4
2
4
5
1
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5
2
-
-
-
-
-
-
7
-
1
-
-
3
4
-
4
-
5
-
4
9
2
-
-
-
1
1
-
4
2
4
5
1
-
-
5
2
-
-
-
-
-
-
-
-
-
289014
Nucci
Interaction of the high-affini ...
Equus asinus
Arch. Biochem. Biophys.
310
49-53
1994
2
1
-
-
-
-
3
1
-
-
-
1
-
1
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289017
Moore
Identification of a site neces ...
Escherichia virus T4, Homo sapiens
Biochemistry
33
2104-2112
1994
3
-
2
-
1
-
6
-
-
1
-
2
-
2
-
-
1
2
-
-
-
-
4
2
2
-
-
-
-
-
-
-
-
-
-
3
-
2
-
-
1
-
-
6
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
289018
Maley
Properties of an affinity-colu ...
Homo sapiens
Biochim. Biophys. Acta
1162
161-170
1993
2
-
1
-
-
5
11
-
-
7
2
1
-
3
-
-
1
1
-
1
1
1
10
1
1
-
-
1
2
-
-
-
-
-
-
2
-
1
-
-
-
5
-
11
-
-
-
7
2
1
-
-
-
1
-
1
1
1
10
1
1
-
-
1
2
-
-
-
-
-
-
-
-
-
289016
Xu
Modulation of deoxycytidylate ...
Homo sapiens
Biochem. Pharmacol.
44
1819-1827
1992
1
1
-
-
-
-
7
-
-
-
-
2
-
2
-
-
1
1
-
3
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
7
-
-
-
-
-
2
-
-
-
1
-
3
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289012
Nucci
Allosteric modifier and substr ...
Equus asinus
Arch. Biochem. Biophys.
289
19-25
1991
2
-
-
-
-
1
4
1
-
-
2
1
-
3
-
-
1
1
-
3
1
1
2
1
1
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
4
-
1
-
-
2
1
-
-
-
1
-
3
1
1
2
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
289013
Whitehead
Hill coefficient ratios give b ...
Equus asinus
Arch. Biochem. Biophys.
289
12-18
1991
2
-
-
-
-
-
2
1
-
-
-
1
-
1
-
-
1
1
-
1
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
1
-
1
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
289019
Riva
-
Correlation between deoxycytid ...
Homo sapiens
J. Cell. Pharmacol.
1
79-85
1990
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289020
Maley
A tale of two enzymes, deoxycy ...
Bacillus subtilis, Enterobacteria phage T2, Enterobacteria phage T6, Equus asinus, Escherichia virus T4, Gallus gallus, Herpes simplex virus, Homo sapiens, Macaca mulatta polyomavirus 1, no activity in Escherichia coli, no activity in Salmonella typhimurium, Polyomavirus sp., Rattus norvegicus, Saccharomyces cerevisiae, Sea urchin
Prog. Nucleic Acid Res. Mol. Biol.
39
49-80
1990
10
3
1
1
-
6
8
8
-
-
1
28
-
15
-
-
2
8
-
20
1
-
70
7
2
-
-
-
-
-
-
-
-
-
-
10
3
1
-
1
-
6
-
8
-
8
-
-
1
28
-
-
-
2
-
20
1
-
70
7
2
-
-
-
-
-
-
-
-
-
-
-
-
-
288997
Maley
Probing the infra-structure of ...
Enterobacteria phage T2, Gallus gallus
Adv. Enzyme Regul.
22
413-430
1984
3
-
-
1
-
-
-
2
-
-
-
8
-
5
-
-
1
2
-
1
-
-
10
2
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
2
-
-
-
8
-
-
-
1
-
1
-
-
10
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289000
McIntosh
Isolation of a Saccharomyces c ...
no activity in Escherichia coli, no activity in Salmonella typhimurium, Saccharomyces cerevisiae
J. Bacteriol.
158
644-649
1984
1
-
-
-
-
-
-
2
-
1
-
1
-
5
-
-
1
-
-
-
-
1
9
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
1
-
1
-
-
-
1
-
-
-
1
9
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
209853
Neale
Enzymes of pyrimidine deoxyrib ...
Mycoplasma mycoides
J. Bacteriol.
156
1001-1005
1983
1
-
-
-
-
1
1
2
-
-
-
1
-
3
-
-
-
1
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
289002
Mastrantonio
Analysis of competition for su ...
Equus asinus
Eur. J. Biochem.
137
421-427
1983
2
-
-
-
-
-
3
3
-
-
1
1
-
2
-
-
-
1
-
2
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
3
-
3
-
-
1
1
-
-
-
-
-
2
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289003
Raia
Reversal of the effect of the ...
Equus asinus
J. Mol. Biol.
157
557-570
1982
5
-
-
-
-
1
8
2
-
-
1
1
-
1
-
-
1
1
-
1
3
-
15
1
1
-
-
-
1
-
-
-
-
-
-
5
-
-
-
-
-
1
-
8
-
2
-
-
1
1
-
-
-
1
-
1
3
-
15
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
288999
Ellims
Deoxycytidylate deaminase. Pur ...
Homo sapiens
J. Biol. Chem.
256
6335-6340
1981
7
-
-
-
-
3
16
1
-
4
2
2
-
2
-
-
1
1
-
2
1
1
8
1
1
-
-
-
3
-
-
-
-
-
-
7
-
-
-
-
-
3
-
16
-
1
-
4
2
2
-
-
-
1
-
2
1
1
8
1
1
-
-
-
3
-
-
-
-
-
-
-
-
-
288998
Nucci
Freezing of dCMP aminohydrolas ...
Equus asinus
J. Mol. Biol.
124
133-145
1978
2
-
-
-
-
-
3
1
-
1
2
1
-
1
-
-
1
1
-
1
2
-
6
1
1
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
3
-
1
-
1
2
1
-
-
-
1
-
1
2
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
289004
Maley
Deoxycytidylate deaminase from ...
Enterobacteria phage T2, no activity in Escherichia coli
Methods Enzymol.
51
412-418
1978
2
-
-
-
-
3
1
4
-
4
1
2
-
3
-
-
1
1
-
-
1
1
12
1
-
-
1
-
3
-
-
-
-
-
-
2
-
-
-
-
-
3
-
1
-
4
-
4
1
2
-
-
-
1
-
-
1
1
12
1
-
-
1
-
3
-
-
-
-
-
-
-
-
-
289005
Mollgaard
Deoxycytidylate deaminase from ...
Bacillusphage phiE, Bacillus subtilis, Bacillus subtilis ED40, bacteriophage SP8, no activity in Escherichia coli, no activity in Salmonella typhimurium
J. Biol. Chem.
253
3536-3542
1978
9
-
-
-
-
4
2
2
-
10
1
2
-
7
-
-
1
1
-
-
1
3
12
-
1
-
2
-
1
1
-
-
-
-
-
9
-
-
-
-
-
4
-
2
-
2
-
10
1
2
-
-
-
1
-
-
1
3
12
-
1
-
2
-
1
1
-
-
-
-
-
-
-
-
289006
Dosseva.I.M.; Tomov
-
Stabilizing effect of ethylene ...
Mus musculus
Dokl. Bolg. Akad. Nauk
28
241-244
1975
-
-
-
-
-
5
-
-
-
-
-
1
-
1
-
-
1
1
-
-
-
-
2
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
289007
Rolton
Deoxycytidylate deaminase. Evi ...
Cricetinae, Herpes simplex virus
Biochem. J.
143
403-409
1974
6
-
-
-
-
3
6
4
-
2
-
2
-
2
-
-
2
-
-
2
-
-
4
-
2
-
4
-
2
-
-
-
-
-
-
6
-
-
-
-
-
3
-
6
-
4
-
2
-
2
-
-
-
2
-
2
-
-
4
-
2
-
4
-
2
-
-
-
-
-
-
-
-
-
289008
Rolton
Deoxycytidylate deaminase. Pro ...
Cricetinae
Biochem. J.
141
211-217
1974
1
-
-
-
-
3
2
1
-
3
2
1
-
1
-
-
1
1
-
2
1
2
4
-
1
-
2
-
1
1
-
1
-
-
-
1
-
-
1
-
-
3
-
2
-
1
-
3
2
1
-
-
-
1
-
2
1
2
4
-
1
-
2
-
1
1
-
-
-
-
-
-
-
-
289009
Maley
T2r+ bacteriophage-induced enz ...
Enterobacteria phage T2, Escherichia virus T4, Gallus gallus
J. Biol. Chem.
247
931-939
1972
5
-
-
-
-
2
3
4
-
-
1
3
-
3
-
-
2
3
-
1
1
2
11
3
2
-
-
-
4
-
-
-
-
-
-
5
-
-
-
-
-
2
-
3
-
4
-
-
1
3
-
-
-
2
-
1
1
2
11
3
2
-
-
-
4
-
-
-
-
-
-
-
-
-
289010
Maley
T2r+ bacteriophage-induced enz ...
Enterobacteria phage T2, Gallus gallus
J. Biol. Chem.
247
940-945
1972
3
-
-
-
-
2
3
-
-
-
2
2
-
2
-
-
-
2
1
1
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
3
-
-
-
-
2
2
-
-
-
-
1
1
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
289011
Sergott
On the regulation of a bacteri ...
Lactobacillus acidophilus, Staphylococcus aureus
J. Biol. Chem.
246
7755-7758
1971
4
-
-
-
-
1
6
-
-
-
-
2
-
2
-
-
2
2
-
-
1
1
4
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
6
-
-
-
-
-
2
-
-
-
2
-
-
1
1
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-