BRENDA - Enzyme Database
show all sequences of 3.5.4.12

Deoxycytidylate deaminase. Properties of the enzyme from cultured kidney cells of baby hamster

Rolton, H.A.; Keir, H.M.; Biochem. J. 141, 211-217 (1974)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dCTP
maximum activation at 0.04 mM, dCTP activation requires presence of Mg2+ or Mn2+; positive allosteric effector
Cricetinae
General Stability
General Stability
Organism
dCTP and Mg2+ stabilize
Cricetinae
dCTP, 0.125 mM, or ethyleneglycol, 20% v/v, stabilize
Cricetinae
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
Cricetinae
Inhibitors
Inhibitors
Commentary
Organism
Structure
dTTP
allosteric inhibitor; maximum inhibition at 0.015 mM, inhibition requires presence of Mg2+ or Mn2+
Cricetinae
EDTA
1 mM: 90% inhibition, restored to maximum by 1-5 mM Mg2+ or Mn2+
Cricetinae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.91
-
dCMP
-
Cricetinae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
dCTP activation and dTTP inhibition requires presence of Mg2+ or Mn2+; required for activation by dCTP and for inhibition by dTTP; required for activation by dCTP, Mg2+ in the absence of dCTP: no effect; required for complete activation by dCTP
Cricetinae
Mn2+
dCTP activation and dTTP inhibition requires presence of Mg2+ or Mn2+
Cricetinae
additional information
bound bivalent metal cations probably present; metal ions not required
Cricetinae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
115000
-
BHK-21/C13 cells, sucrose density gradient centrifugation
Cricetinae
130000
-
BHK-21/C13 cells, gel filtration
Cricetinae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Cricetinae
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
Cricetinae
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cricetinae
-
BHK-21/C13 cells, baby-hamster
-
Purification (Commentary)
Commentary
Organism
partial, BHK-21/C13 cells, baby-hamster
Cricetinae
Reaction
Reaction
Commentary
Organism
dCMP + H2O = dUMP + NH3
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
Cricetinae
Source Tissue
Source Tissue
Commentary
Organism
Textmining
BHK-21 cell
baby-hamster kidney
Cricetinae
-
kidney
BHK-21/C13 cells, baby-hamster kidney cells
Cricetinae
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.37
-
-
Cricetinae
Storage Stability
Storage Stability
Organism
-70C
Cricetinae
-70C, 20% v/v ethyleneglycol, stable for 2 months
Cricetinae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-hydroxymethyl-dCMP + H2O
-
289008
Cricetinae
5-hydroxymethyl-dUMP + NH3
-
-
-
?
5-methyl-dCMP + H2O
-
289008
Cricetinae
5-methyl-dUMP + NH3
-
-
-
?
dCMP + H2O
-
289008
Cricetinae
dUMP + NH3
-
289008
Cricetinae
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289008
Cricetinae
dUMP + NH3
-
289008
Cricetinae
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Cricetinae
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
Cricetinae
50
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and Mg2+, or by increasing protein concentration
Cricetinae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
BHK-21/C13 cells
Cricetinae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
9
pH 7.0: 60%, pH 8.2: 98% and pH 9.0 96% of maximum activity
Cricetinae
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no coenzyme required
Cricetinae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dCTP
maximum activation at 0.04 mM, dCTP activation requires presence of Mg2+ or Mn2+; positive allosteric effector
Cricetinae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no coenzyme required
Cricetinae
General Stability (protein specific)
General Stability
Organism
dCTP and Mg2+ stabilize
Cricetinae
dCTP, 0.125 mM, or ethyleneglycol, 20% v/v, stabilize
Cricetinae
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
Cricetinae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dTTP
allosteric inhibitor; maximum inhibition at 0.015 mM, inhibition requires presence of Mg2+ or Mn2+
Cricetinae
EDTA
1 mM: 90% inhibition, restored to maximum by 1-5 mM Mg2+ or Mn2+
Cricetinae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.91
-
dCMP
-
Cricetinae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
dCTP activation and dTTP inhibition requires presence of Mg2+ or Mn2+; required for activation by dCTP and for inhibition by dTTP; required for activation by dCTP, Mg2+ in the absence of dCTP: no effect; required for complete activation by dCTP
Cricetinae
Mn2+
dCTP activation and dTTP inhibition requires presence of Mg2+ or Mn2+
Cricetinae
additional information
bound bivalent metal cations probably present; metal ions not required
Cricetinae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
115000
-
BHK-21/C13 cells, sucrose density gradient centrifugation
Cricetinae
130000
-
BHK-21/C13 cells, gel filtration
Cricetinae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Cricetinae
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
dUMP + NH3
-
Cricetinae
?
Purification (Commentary) (protein specific)
Commentary
Organism
partial, BHK-21/C13 cells, baby-hamster
Cricetinae
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
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.37
-
-
Cricetinae
Storage Stability (protein specific)
Storage Stability
Organism
-70C
Cricetinae
-70C, 20% v/v ethyleneglycol, stable for 2 months
Cricetinae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-hydroxymethyl-dCMP + H2O
-
289008
Cricetinae
5-hydroxymethyl-dUMP + NH3
-
-
-
?
5-methyl-dCMP + H2O
-
289008
Cricetinae
5-methyl-dUMP + NH3
-
-
-
?
dCMP + H2O
-
289008
Cricetinae
dUMP + NH3
-
289008
Cricetinae
?
dCMP + H2O
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
289008
Cricetinae
dUMP + NH3
-
289008
Cricetinae
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Cricetinae
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
Cricetinae
50
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and Mg2+, or by increasing protein concentration
Cricetinae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
BHK-21/C13 cells
Cricetinae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
9
pH 7.0: 60%, pH 8.2: 98% and pH 9.0 96% of maximum activity
Cricetinae
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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2
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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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2
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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
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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1
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688405
Hou
Crystal structures of Streptoc ...
Streptococcus mutans
J. Mol. Biol.
377
220-231
2008
1
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1
1
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1
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5
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1
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2
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1
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1
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2
2
1
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1
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-
686248
Liskay
Involvement of deoxycytidylate ...
Saccharomyces cerevisiae
Curr. Biol.
17
R755-R757
2007
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2
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1
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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
2
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5
1
2
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4
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1
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1
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1
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1
4
1
1
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
1
1
1
1
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2
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669680
Gribaudo
Human cytomegalovirus requires ...
Homo sapiens
J. Gen. Virol.
84
1437-1441
2003
1
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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
1
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1
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1
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3
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6
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4
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1
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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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1
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1
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4
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1
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3
1
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2
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1
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1
-
-
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-
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668584
Jost
5-Methyldeoxycytidine monophos ...
Homo sapiens
FEBS Lett.
519
128-134
2002
1
-
-
-
-
-
1
1
-
1
-
3
-
2
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1
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2
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5
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1
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1
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1
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1
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1
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1
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3
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1
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2
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5
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1
-
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1
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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
-
4
-
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1
3
1
-
4
2
4
5
1
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5
2
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7
-
1
-
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3
4
-
4
-
5
-
4
9
2
-
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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
-
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1
-
1
-
-
1
1
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1
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1
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1
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1
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1
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1
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1
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-
-
-
289017
Moore
Identification of a site neces ...
Escherichia virus T4, Homo sapiens
Biochemistry
33
2104-2112
1994
3
-
2
-
1
-
6
-
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1
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2
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2
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1
2
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4
2
2
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6
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1
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4
2
2
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289018
Maley
Properties of an affinity-colu ...
Homo sapiens
Biochim. Biophys. Acta
1162
161-170
1993
2
-
1
-
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5
11
-
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7
2
1
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3
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1
1
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1
1
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10
1
1
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1
2
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1
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5
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11
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7
2
1
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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
-
-
-
-
-
-
-
-
-
-
-
-
-