Information on EC 3.5.4.12 - dCMP deaminase

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The expected taxonomic range for this enzyme is: Bacilli

EC NUMBER
COMMENTARY
3.5.4.12
-
RECOMMENDED NAME
GeneOntology No.
dCMP deaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dCMP + H2O = dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
mechanism; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; mechanism; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; mechanism; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; mechanism; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; most dramatic allosteric response at substrate levels 0.1 mM dCMP or less; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
feedback regulation; highly regulated allosteric enzyme; regulation, allosteric end-product regulation
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
zinc ion-based reaction mechanism, substrate binding structure
-
dCMP + H2O = dUMP + NH3
show the reaction diagram
highly regulated allosteric enzyme; regulation, allosteric end-product regulation
Bacillus subtilis ED40
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of amidines
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
pyrimidine deoxyribonucleotides biosynthesis from CTP
-
Pyrimidine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
dCMP aminohydrolase
Also acts on some 5-substituted dCMPs.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-deoxycytidylate deaminase
-
-
2-deoxycytidylate deaminase
-
-
5-mdCMP deaminase
-
-
5-methyldeoxycytidine monophosphate deaminase
-
-
dCMP deaminase
-
-
-
-
dCMP deaminase
-
-
dCMP deaminase
-
-
dCMP-aminohydrolase
-
-
-
-
dCMP-dCTP deaminase
O41078
-
dCMPase
-
-
-
-
dCMPD
-
-
-
-
deaminase, deoxycytidylate
-
-
-
-
deoxy-CMP-deaminase
-
-
-
-
deoxycytidine deaminase
-
-
deoxycytidine monophosphate deaminase
-
-
-
-
deoxycytidine monophosphate deaminase
-
-
deoxycytidine nucleotide deaminase
-
-
-
-
deoxycytidine-5'-monophosphate aminohydrolase
-
-
-
-
deoxycytidine-5'-phosphate deaminase
-
-
-
-
deoxycytidine-5?-monophosphate deaminase
-
-
deoxycytidylate aminohydrolase
-
-
-
-
deoxycytidylate deaminase
-
-
-
-
deoxycytidylate deaminase
-
-
deoxycytidylate deaminase
-
-
deoxycytidylate deaminase
-
-
T2-dCMP deaminase
-
T2-phage infected
T2-deoxycytidylate deaminase
-
T2-phage infected
T2-phage deoxycytidylate deaminase
-
T2-phage infected
T4-dCMP deaminase
-
T4-phage infected
T4-deaminase
-
T4-phage infected
T4-phage deoxycytidylate deaminase
-
T4-phage infected
CAS REGISTRY NUMBER
COMMENTARY
9026-92-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ED40
-
-
Manually annotated by BRENDA team
Bacillus subtilis ED40
strain ED40
-
-
Manually annotated by BRENDA team
host Bacillus subtilis
-
-
Manually annotated by BRENDA team
bacteriophage SP8
host Bacillus subtilis
-
-
Manually annotated by BRENDA team
BHK-21/C13 cells, baby-hamster
-
-
Manually annotated by BRENDA team
BHK-21/C13 cells, baby-hamster, enzyme from non-infected cells and cells infected by Herpes simplex
-
-
Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli
-
-
Manually annotated by BRENDA team
T2-phage infected Escherichia coli
-
-
Manually annotated by BRENDA team
T2-phage infected Escherichia coli; T2r+-infected Escherichia coli B; T2-, T4-, and T6-phage induced enzyme in Escherichia coli
-
-
Manually annotated by BRENDA team
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
-
-
Manually annotated by BRENDA team
T2r+-infected Escherichia coli B
-
-
Manually annotated by BRENDA team
; T2-, T4-, and T6-phage induced enzyme in Escherichia coli; T4-phage infected Escherichia coli; wild-type and R115E and R115Q, mutant enzymes that no longer requires dCTP for activation, and mutant F112A
-
-
Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli; T4-phage infected Escherichia coli
-
-
Manually annotated by BRENDA team
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
-
-
Manually annotated by BRENDA team
T4-phage infected Escherichia coli; wild-type and mutant F112A
-
-
Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli
-
-
Manually annotated by BRENDA team
donkey; three conformational isomers of dCMPase, the conformation of the enzyme with no ligands, the activated form, R form: dCTP-Mg complex and the inhibited form, T form: dTTP-Mg complex
-
-
Manually annotated by BRENDA team
Herpes simplex virus
host baby-hamster, BHK-21/C13 cells; induced by
-
-
Manually annotated by BRENDA team
Herpes simplex virus
induced by
-
-
Manually annotated by BRENDA team
human; patients with acute nonlymphocytic leukemia
-
-
Manually annotated by BRENDA team
Ehrlich's ascites tumor cells and various gastrointestinal tumors
-
-
Manually annotated by BRENDA team
subsp. mycoides
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
enzyme not detectable in Escherichia coli until after infection with T-even bacteriophage
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
enzyme not detectable in Escherichia coli until after infection with T-even bacteriophage; wild type Escherichia coli contains no dCMP deaminase
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
wild type Escherichia coli contains no dCMP deaminase
-
-
Manually annotated by BRENDA team
no activity in Salmonella typhimurium
-
-
-
Manually annotated by BRENDA team
no activity in Salmonella typhimurium
do not contain dCMP deaminase
-
-
Manually annotated by BRENDA team
i.e. PBCV-1 , a chlorovirus from host Chlorella sp. strain NC64A
SwissProt
Manually annotated by BRENDA team
induced by
-
-
Manually annotated by BRENDA team
Sea urchin
-
-
-
Manually annotated by BRENDA team
induced by
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
dCMPD is pivotal in deoxyuridine analogs nucleotide formation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-FTCMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',2'-difluoro-dCMP + H2O
2',2'-difluoro-dUMP + NH3
show the reaction diagram
-
-
-
-
?
2',3'-dideoxy-5-fluoro-3'-thiacytidine + H2O
?
show the reaction diagram
-
good substrate
-
-
?
5-aza-dCMP + H2O
5-aza-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-bromo-dCMP + H2O
5-bromo-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-bromo-dCMP + H2O
5-bromo-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-bromo-dCMP + H2O
5-bromo-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-bromo-dCMP + H2O
5-bromo-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-bromo-dCMP + H2O
5-bromo-dUMP + NH3
show the reaction diagram
-
very good substrate
-
-
?
5-chloro-dCMP + H2O
5-chloro-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-chloro-dCMP + H2O
5-chloro-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-fluoro-dCMP + H2O
5-fluoro-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-fluoro-dCMP + H2O
5-fluoro-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-fluoro-dCMP + H2O
5-fluoro-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-fluoro-dCMP + H2O
5-fluoro-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-fluoro-dCMP + H2O
5-fluoro-dUMP + NH3
show the reaction diagram
-
very good substrate
-
-
?
5-Hg-dCMP + H2O
5-Hg-dUMP + NH3
show the reaction diagram
-
very poor substrate in the absence of mercaptoethanol, deamination activated by dTTP and inhibited by dCTP
-
-
?
5-Hg-dCMP + H2O
5-Hg-dUMP + NH3
show the reaction diagram
-
deamination activated by dTTP and inhibited by dCTP
-
-
?
5-Hg-dCMP + H2O
5-Hg-dUMP + NH3
show the reaction diagram
-
deamination activated by dTTP and inhibited by dCTP
-
-
?
5-Hg-dCMP + H2O
5-Hg-dUMP + NH3
show the reaction diagram
-
5-mercury derivative of dCMP only in the presence of an excess of mercaptoethanol
-
-
?
5-Hg-dCMP + H2O
5-Hg-dUMP + NH3
show the reaction diagram
-
5-mercury derivative of dCMP only in the presence of an excess of mercaptoethanol
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
not a substrate
-
-
?
5-hydroxymethyl-dCMP + H2O
5-hydroxymethyl-dUMP + NH3
show the reaction diagram
-
HeLa cells, good substrate
-
-
?
5-iodo-dCMP + H2O
5-iodo-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-iodo-dCMP + H2O
5-iodo-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-iodo-dCMP + H2O
5-iodo-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-iodo-dCMP + H2O
5-iodo-dUMP + NH3
show the reaction diagram
-
very poor substrate
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
-
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
very good substrate
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
5-methyl-dCMP: very poor substrate
-
-
?
5-methyl-dCMP + H2O
5-methyl-dUMP + NH3
show the reaction diagram
-
HeLa cells, good substrate
-
-
?
5-methyl-dCMP + H2O
dTMP + NH3
show the reaction diagram
-
-, deamination pathway, overview
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
not a substrate
-
-
-
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
deaminated only in the presence of dCTP, strongly activated by dCTP
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
arabinosyl-CMP
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
arabinosyl-CMP
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
at a very low rate
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
1-beta-D-arabinofuranosyl-CMP, effective substrate in presence of dCTP
-
-
?
ara-CMP + H2O
ara-UMP + NH3
show the reaction diagram
-
effective substrate in presence of dCTP
-
-
?
ara-CMP+ H2O
?
show the reaction diagram
-
fair substrate
-
-
?
beta-D-2',2'-difluorodeoxycytidine + H2O
beta-D-2',2'-difluorodeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
-
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
-
-
-
-
CMP + H2O
UMP + NH3
show the reaction diagram
-
-
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
poor substrate
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
poor substrate
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
slight activity, about 5% compared with dCMP
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
deaminated only in the presence of dCTP, strongly activated by dCTP
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
at a low rare, strongly activated by dCTP
-
-
?
CMP + H2O
UMP + NH3
show the reaction diagram
-
HeLa cells, at 1 mM, in presence and absence of dCTP and Mg2+: not a substrate
-
-
-
CMP + H2O
UMP + NH3
show the reaction diagram
Bacillus subtilis ED40
-
slight activity, about 5% compared with dCMP
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Sea urchin
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Equus asinus, Herpes simplex virus
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Bacillusphage phiE, bacteriophage SP8
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
O41078, -
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
O41078, -
-
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
most dramatic allosteric response at substrate levels 0.1 mM dCMP or less
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
high degree of specificity of dCMP
-
ir
dCMP + H2O
dUMP + NH3
show the reaction diagram
Herpes simplex virus, Cricetinae
-
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
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
true substrate probably dCMP-Mg complex
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
highly specific for dCMP
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
not a substrate of the T form, dTTP-induced form of the enzyme
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Herpes simplex virus, Cricetinae
-
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme of pyrimidine deoxyribonucleotide metabolism, important for the synthesis of thymidine nucleotides from thymine. Enzyme could provide the major means of dUMP formation
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme involved in formation of dTMP
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
one of the regulatory enzymes of DNA biosynthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme contributes formation of DNA by providing dUMP as substrate for thymidylate synthase. Potential role in cell division
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
catalyzed reaction is at a branching point of the pathway leading to dCTP and dTTP, immediate pyrimidine deoxynucleotide precursors in DNA biosynthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
key enzyme in pyrimidine deoxyribonucleotide metabolism, catalyzing the rate-limiting step, plays an important role in providing a balanced supply of dCTP and dTTP for DNA synthesis
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme within pyrimidine deoxynucleotide pathway
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
important role in regulation of intracellular TTP levels
-
-
ir
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme plays an important if not rate controlling step in cell division
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
regulating dTMP for DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
pathway for synthesis of dUMP, nucleotide required for synthesis of dTMP
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
critical branchpoint in pyrimidine deoxynucleotide metabolism
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme is major source of mammalian cell dUMP pool and regulates the synthesis of TMP
-
-
ir
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
deoxycytidine nucleotides are shunted into dTMP biosynthetic pathway via reaction catalyzed by dCMP deaminase
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme is important in the de novo synthesis of thymidine nucleotides, and may also be involved in the metabolism of anticancer agents
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme is the major supplier of substrate for the thymidylate synthase important in DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme plays a key role in the thymidylate synthase, pathway overview
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview, a conserved motif, G43YNG46, is involved in the binding of dCTP, N-terminal Arg4, a key residue located between two monomers, binds strongly to the gamma phosphate group of dCTP, active site structure and substrate binding, overview
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Bacillus subtilis ED40
-
-, importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
?
dCMP-Hg-S-CH2-CH2-OH + H2O
dUMP-Hg-S-CH2-CH2-OH + NH3
show the reaction diagram
-
better substrate of T form: in the presence of dTTP
-
-
?
dCTP + H2O
dUTP + NH3
show the reaction diagram
O41078, -
-
-
-
?
PSI-6130-MP + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-, the enzyme is a key enzyme in the inactivation of deoxycytidine and several chemotherapeutically important nucleoside analogues
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
halogenated deoxycytidylates: very poor substrates
-
-
-
additional information
?
-
-
HeLa cells, no activity with CDP at 1 mM, in presence and absence of dCTP and Mg2+
-
-
-
additional information
?
-
-
no activity with dCDP, dCTP, CDP, CTP
-
-
-
additional information
?
-
-
catalyzes deamination of halogenated derivatives of dCMP, but appears to be restricted in its ability to deaminate substrates with a large group in the 5-position
-
-
-
additional information
?
-
-
function of enzyme is that of enhancing stability of T4-phage multienzyme complex involved in dNTP synthesis, the complex is less stable in cd mutants
-
-
-
additional information
?
-
-
enzyme is involved in elimination of some dCyd analogues, such as 2',2'-difluorodeoxycytidine, fluoro-dCyd, and ara-C, from tissues or cultured cells
-
-
-
additional information
?
-
-
the enzyme also performs 5-methylcytidyl-DNA deaminase activity but to a lesser extent, deamination pathway, overview
-
-
-
additional information
?
-
-
the human cytomegalovirus requires the cellular host dCMP deaminase for replication in quiescent cells, overview
-
-
-
additional information
?
-
-
substrate specificity with deoxycytidine analogue monophosphates, overview
-
-
-
additional information
?
-
-
the enzyme also performs 5-methylcytidyl-DNA deaminase activity but to a lesser extent, substrate specificity, overview
-
-
-
additional information
?
-
O41078, -
the bifunctional dCMP-dCTP deaminase shows dCMP deaminase and dCTP deaminase activities, dCTP serves as a positive heterotropic effector for the dCMP deaminase activity and a positive homotropic effector for the dCTP deaminase activity, and the enzymatic efficiency of the dCMP deaminase activity is about four times higher than that of the dCTP deaminase activity, the same active site is involved in both dCMP and dCTP deaminations
-
-
-
additional information
?
-
-
cytidine monophosphate is not a good substrate for dCMPD. Monophosphates of deoxycytidine analogs nucleosides in the L-conformation (e.g. apricitabine, lamivudine, and emtricitabine) and dideoxycytidine do not act as substrates of dCMPD
-
-
-
additional information
?
-
Bacillus subtilis ED40
-
substrate specificity, no activity with dCDP, dCTP, CDP, CTP
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-methyl-dCMP + H2O
dTMP + NH3
show the reaction diagram
-
deamination pathway, overview
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
O41078, -
-
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
true substrate probably dCMP-Mg complex
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Herpes simplex virus, Cricetinae
-
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme involved in main pathway leading to synthesis of dTTP, role in provision of precursors for DNA synthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme of pyrimidine deoxyribonucleotide metabolism, important for the synthesis of thymidine nucleotides from thymine. Enzyme could provide the major means of dUMP formation
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme involved in formation of dTMP
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
one of the regulatory enzymes of DNA biosynthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme contributes formation of DNA by providing dUMP as substrate for thymidylate synthase. Potential role in cell division
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
catalyzed reaction is at a branching point of the pathway leading to dCTP and dTTP, immediate pyrimidine deoxynucleotide precursors in DNA biosynthesis
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
providing an adequate supply of dUMP for formation of dTMP, via dTMP synthase a crucial intermediate for synthesis of DNA
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
key enzyme in pyrimidine deoxyribonucleotide metabolism, catalyzing the rate-limiting step, plays an important role in providing a balanced supply of dCTP and dTTP for DNA synthesis
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme within pyrimidine deoxynucleotide pathway
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
important role in regulation of intracellular TTP levels
-
-
ir
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme plays an important if not rate controlling step in cell division
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
regulating dTMP for DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
pathway for synthesis of dUMP, nucleotide required for synthesis of dTMP
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
critical branchpoint in pyrimidine deoxynucleotide metabolism
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
-
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
enzyme is major source of mammalian cell dUMP pool and regulates the synthesis of TMP
-
-
ir
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
deoxycytidine nucleotides are shunted into dTMP biosynthetic pathway via reaction catalyzed by dCMP deaminase
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme is important in the de novo synthesis of thymidine nucleotides, and may also be involved in the metabolism of anticancer agents
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme is the major supplier of substrate for the thymidylate synthase important in DNA synthesis
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the enzyme plays a key role in the thymidylate synthase, pathway overview
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
-
the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview
-
-
?
dCMP + H2O
dUMP + NH3
show the reaction diagram
Bacillus subtilis ED40
-
importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides
-
?
dCTP + H2O
dUTP + NH3
show the reaction diagram
O41078, -
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
the enzyme is a key enzyme in the inactivation of deoxycytidine and several chemotherapeutically important nucleoside analogues
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
function of enzyme is that of enhancing stability of T4-phage multienzyme complex involved in dNTP synthesis, the complex is less stable in cd mutants
-
-
-
additional information
?
-
-
enzyme is involved in elimination of some dCyd analogues, such as 2',2'-difluorodeoxycytidine, fluoro-dCyd, and ara-C, from tissues or cultured cells
-
-
-
additional information
?
-
-
the enzyme also performs 5-methylcytidyl-DNA deaminase activity but to a lesser extent, deamination pathway, overview
-
-
-
additional information
?
-
-
the human cytomegalovirus requires the cellular host dCMP deaminase for replication in quiescent cells, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no coenzyme required
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation of enzyme by dCTP or inhibition by TTP has absolute requirement for the presence of a divalent cation. Mg2+, Ca2+ and Mn2+ are equally effective cations for enzyme activation by dCTP, Mn2+ and Ca2+ are more effective than Mg2+ in enzyme inhibition by TTP
Ca2+
-
reaction completely dependent on divalent cations, most effective Mg2+, Mn2+ and Ca2+ less effective than Mg2+
Ca2+
-
no activation
Ca2+
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
Ca2+
-
can partially substitute for Mg2+, 50% of the activity with Mg2+
Ca2+
O41078, -
can partially substitute for Mg2+
Co2+
-
metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+
Co2+
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
Divalent cations
-
reaction completely dependent on divalent cations
Divalent cations
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
metal ion
-
required, in the absence of metal ions: 40% activity, Zn2+ highest activity, around 20% activity with Co2+, Mn2+, and Ni2+, no activity in the presence of Mg2+, Ca2+ and Fe2+
Mg2+
-
required for activation by dCTP and for inhibition by dTTP
Mg2+
-
activation of enzyme by dCTP or inhibition by TTP has absolute requirement for the presence of a divalent cation. Mg2+, Ca2+ and Mn2+ are equally effective cations for enzyme activation by dCTP, Mn2+ and Ca2+ are more effective than Mg2+ in enzyme inhibition by TTP
Mg2+
-
required for activation by dCTP, Mg2+ in the absence of dCTP: no effect
Mg2+
-
reaction completely dependent on divalent cations, most effective Mg2+, Mn2+ and Ca2+ less effective than Mg2+
Mg2+
-
enzyme requires dCTP, Zn2+, and 2-mercaptoethanol, Mg2+ cannot substitute for Zn2+; no activation
Mg2+
Cricetinae, Herpes simplex virus
-
required for activation by dCTP and for inhibition by dTTP; required for complete activation by dCTP
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
Mg2+
-
required for activation by dCTP and for inhibition by dTTP
Mg2+
-
; required for activation by dCTP and for inhibition by dTTP
Mg2+
-
required for activation by dCTP and for inhibition by dTTP
Mg2+
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective; required for activation by dCTP and for inhibition by dTTP; required for activation by dCTP, Mg2+ in the absence of dCTP: no effect
Mg2+
-
-
Mg2+
-
required for activity, in complex with activator dCTP, can be substituted by Ca2+ or Mn2+, but not by Zn2+, Co2+, Ni2+, and Cu2+
Mg2+
O41078, -
the enzyme depends on divalent cations, Mg2+ is preferred, but can partially be substituted by Ca2+, Ni2+, or Mn2+
Mn2+
-
activation of enzyme by dCTP or inhibition by TTP has absolute requirement for the presence of a divalent cation. Mg2+, Ca2+ and Mn2+ are equally effective cations for enzyme activation by dCTP, Mn2+ and Ca2+ are more effective than Mg2+ in enzyme inhibition by TTP
Mn2+
-
reaction completely dependent on divalent cations, most effective Mg2+, Mn2+ and Ca2+ less effective than Mg2+
Mn2+
-
metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+
Mn2+
-
dCTP activation and dTTP inhibition requires presence of Mg2+ or Mn2+
Mn2+
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
Mn2+
-
can partially substitute for Mg2+, 26% of the activity with Mg2+
Ni2+
-
metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+
Ni2+
O41078, -
can partially substitute for Mg2+
Zn2+
-
required, enzyme requires dCTP, Zn2+, and 2-mercaptoethanol, Mg2+ cannot substitute for Zn2+
Zn2+
-
two resident Zn2+ atoms /subunit
Zn2+
-
involved in catalytic mechanism involving His104, and Cys132 and Cys135
Zn2+
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
Zn2+
-
the enzyme shows a zinc ion-based reaction mechanism, binding structure and coordinating residues, two zinc ions per subunit, the first is coordinated by His104, Cys132, and Cys135, the second by Cys19, Cys49, His94, and Glu102, overview
Zn2+
-
two conserved motifs are involved in the binding of Zn2+, Zn2+ cannot substitute for Mg2+
Zn2+
O41078, -
the enzyme contains a zinc binding site, but shows less than 6% of maximal activity with Zn2+ as divalent cation
Mn2+
O41078, -
can partially substitute for Mg2+
additional information
-
metal ions not required
additional information
-
metal ions not required
additional information
-
metal ion required, in the absence of metal ions: 40% activity, Zn2+ highest activity, around 20% activity with Co2+, Mn2+, and Ni2+, no activity in the presence of Mg2+, Ca2+ and Fe2+
additional information
bacteriophage SP8
-
metal ions not required
additional information
-
bound bivalent metal cations probably present; metal ions not required
additional information
-
divalent cations not necessary to improve activity, activation by dCTP and inhibition by dTTP both show an absolute requirement for a divalent cation. Mg2+, Ca2+ and Mn2+ almost equally effective in promoting activation by dCTP, Cu2+, Zn2+, and Co2+ are ineffective
additional information
-
no metals required
additional information
-
Co2+, Ni2+, and Cu2+ cannot substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
-
decreases the enzyme activity in vivo in transformed NM-16 fibroblasts, but increases it in normal Rat-2 fibroblasts
2',2'-difluoro-dCTP
-
dual mechanism of inhibition; partial purified enzyme
2',2'-difluorodeoxycytidine
-
high cellular nucleotide levels: inhibition: Concentration-dependent inhibition; inhibition by nucleotides of 2',2'-difluorodeoxycytidine, dual mechanism of inhibition
2',3'-di-dTTP
-
7% inhibition
2',3'-dihydro-2',3'-dideoxy-thymidine monophosphate
-
-
2'-beta-D-deoxyribose-pyrimidin-2-one 5'-phosphate
-
competitive inhibition, Ki: 0.000012 mM
2'-deoxythymidine
-
0.05 mM: 60% inhibition, 0.01 mM: 5% inhibition; dThd
3'-azido-2',3'-dideoxy-thymidine monophosphate
-
-
3,4,5,6-tetrahydro-2'-deoxyuridine
-
-
3,4,5,6-tetrahydro-2'-deoxyuridine
-
specifc inhibition
3,4,5,6-tetrahydro-2'-dUMP
-
high-affinity inhibitor, rapid, reversible inhibition, kinetics of inhibition. At low substrate or competitor concentrations: activation. Tetrahydro-dUMP activates enzyme at low substrate concentrations
3,4,5,6-tetrahydro-2'-dUMP
-
specific potent inhibitor
3,4,5,6-tetrahydro-2'-dUMP
-
potent inhibitor, Ki: 0.00001 mM
5-(acryloylamino-pentanol-1)2'-beta-D-dUMP
-
-
-
5-bromo-dUTP
-
92% inhibition
5-fluoro-dUMP
-
-
5-Hg-dCMP
-
irreversible competitive inhibitor, in the absence of mercaptoethanol
5-Hg-dCMP
-
potent inhibitor, in the absence of 2-mercaptoethanol, 0.00024 mM: 37% inhibition, 0.0024 mM: 70% inhibition
5-Hg-dUMP
-
potent inhibitor, 0.0001 mM: 54% inhibition
ADP
-
slight inhibition
AMP
-
slight inhibition, competitive inhibitor, mechanism of inhibition
arabinosylcytosine
-
ara-C, deactivating dCMP deaminase
beta-D-2',2'-difluorodeoxycytidine
-
competitive
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
slight inhibition
beta-L-2',3'-dideoxy-5'-fluoro-3'-thiacytidine monophosphate
-
-
Co2+
-
1 mM: 75% inhibition
Cu2+
-
1 mM: 98% inhibition
D-beta-2'-fluoro-5-methyl-arabinofuranosyluracil monophosphate
-
no inhibition by L-beta-2'-fluoro-5-methyl-arabinofuranosyluracil monophosphate
dAMP
-
at low substrate, dCMP, concentration: activation at higher concentration of either: competitive inhibition; competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate
dAMP
-
competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate
dAMP
-
kinetics of dAMP inhibition
dCTP
-
allosteric activator, 12fold, for aminohydrolysis of dCMP, inhibitor, 50% inhibition, for substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH
dCTP
-
allosteric activator, 12fold, for aminohydrolysis of dCMP, inhibitor, 50% inhibition, for substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH
deoxytetrahydrouridine
-
-
-
deoxythymidine 5'-triphosphate
-
allosteric feedback regulation of the enzyme by products of the metabolic pathway, allosteric regulation involved residues 112 and 115
dGDP
-
slight inhibition
dGMP
-
effective competitive inhibitor, mechanism of inhibition
dGMP
-
competitive inhibitor
dGMP
-
potent competitive inhibitor
dTTP
-
allosteric inhibitor
dTTP
-
0.01 mM: 100% inhibition. In the presence of glutaraldehyde enzyme is less sensitive to inhibitory effect of dTTP; allosteric inhibitor; inhibited form: dTTP-enzyme; kinetics of inhibition
dTTP
-
allosteric inhibitor; allosteric inhibitor, 100% inhibition, for substrate dCMP, becomes activator, 2.5fold, for mercury substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH
dTTP
bacteriophage SP8
-
no inhibition by dTTP
dTTP
Cricetinae, Herpes simplex virus
-
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
dTTP
-
allosteric inhibitor; maximum inhibition at 0.015 mM, inhibition requires presence of Mg2+ or Mn2+
dTTP
-
allosteric inhibitor; inhibition by dTTP increases markedly as the pH is raised, pH-dependent inhibition
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor; specifically markedly inhibited, Ki: 0.0017 mM
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor; cooperative inhibition, reversed by dCTP, mechanism of inhibition
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor; wild-type, 0.1 mM dTTP: 20% inhibition, mutants R115E and R115Q: 0.1 mM dTTP: no inhibition. 0.3 mM dTTP: wild-type 90% inhibition, mutants R115E and R115Q: 30% inhibition
dTTP
-
allosteric inhibitor; mutant F112A, no or very slight inhibition, high concentration, 0.24 mM: slight inhibition
dTTP
-
0.0015 mM: 50% inhibition. dTTP inhibition reversed by dCTP; allosteric inhibitor
dTTP
-
allosteric inhibitor; dTTP favores disaggregated or inhibited state
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor; dTTP favores disaggregated or inhibited state
dTTP
Herpes simplex virus
-
-
dTTP
-
allosteric inhibitor
dTTP
-
allosteric inhibitor
dTTP
-
an allosteric inhibitor
dTTP
O41078, -
inhibits dCMP deamination, feedback inhibition
dTTP
-
inhibits dCMPD by allosteric interaction
dUMP
-
poor competitive inhibitor, mechanism of inhibition
dUMP
-
competitive inhibition, kinetics and mechanism of inhibition
dUMP
-
competitive inhibitor
dUMP
-
product inhibition
dUMP
-
potent competitive inhibitor
dUTP
-
slight inhibition
dUTP
-
79% inhibition
dUTP
-
allosteric inhibitor
EDTA
-
no inhibition by EDTA
EDTA
-
completely
EDTA
-
1 mM: 90% inhibition, restored to maximum by 1-5 mM Mg2+ or Mn2+
Glutaraldehyde
-
25% glutaraldehyde: rapid inhibition; dCTP protects enzyme to a certain extent. Glutaraldehyde fixes dCMPase in the activated conformation induced by dCTP
Glutaraldehyde
-
25% glutaraldehyde: rapid inhibition; substrate dCMP: rapid inhibition, protection by dGMP, or dTTP or both is slight, substrate dCMP-Hg-S-CH2-CH2-OH: 3fold activation
glycerol
-
substrate dCMP: activation, substrate dCMP-Hg-S-CH2-CH2-OH, 20% glycerol: inhibition, removed by dTTP
GMP
-
slight inhibition
GMP
-
potent competitive inhibitor
guanidine hydrochloride
-
0.5 M: 50% inhibition, 1 M: 100% inhibition
H4dUMP
O41078, -
inhibits both dCTP and dCMP deaminase activities
Herpes antiserum
Herpes simplex virus
-
inhibition of Herpes infected-cell enzyme
-
PDRP
O41078, -
inhibits both dCTP and dCMP deaminase activities
pre-immune serum
Herpes simplex virus
-
inhibition of Herpes infected-cell enzyme
-
pyrimidin-2-one deoxyribotide
-
active site binding structure, overview
TDP
-
slight inhibition, competitive inhibitor, mechanism of inhibition
tetrahydrodeoxyuridine
-
-
-
TMP
-
poor competitive inhibitor, mechanism of inhibition
TTP
-
activating enzyme up to 1.7fold at concentration of 0.00025 mM, but inhibiting at higher concentration, 0.015 mM: 85% inhibition; inhibition by TTP has absolute requirement for the presence of a divalent cation, Mn2+ and Ca2+ are more effective than Mg2+ in the inhibition of enzyme activity by TTP; TTP inhibition partially reversed by dCTP
TTP
-
inhibits dCMPD by allosteric interaction
UTP
-
slight inhibition
UTP-adipic hydrazide
-
cooperative inhibition, reversed by dCTP
zebularine
-
-
Zn2+
-
1 mM: 94% inhibition
Hg(CH3COO)2
-
Hg(acetate)2; mercuroacetate, potent inhibitor, 0.0002 mM: 26% inhibition, 0.001 mM: 40% inhibition
additional information
-
no inhibition by EDTA
-
additional information
Cricetinae, Herpes simplex virus
-
no inhibition by KCl up to 0.3 M
-
additional information
-
no inhibition by dATP, dGTP, 5-bromo-UTP
-
additional information
-
mechanism of inhibition
-
additional information
-
kinetics of inhibition; mechanism of inhibition
-
additional information
-
little or no inhibition by 3,4,5,6-tetrahydrouridine; mechanism of inhibition
-
additional information
-
no inhibition by deoxynucleotide triphosphates
-
additional information
-
inhibitory potency of pyrimidine phosphate analogues, overview
-
additional information
-
monophosphates of deoxycytidine analogs nucleosides in the L-conformation (e.g. apricitabine, lamivudine, and emtricitabine) and dideoxycytidine do not act as inhibitors of dCMPD
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
-
increases the enzyme activity in vivo in normal Rat-2 fibroblasts, but decreases it in transformed NM-16 fibroblasts
1-beta-D-arabinofuranosylcytosine 5'-triphosphate
-
low activation, allosteric activator
2-mercaptoethanol
-
enzyme requires dCTP, Zn2+, and 2-mercaptoethanol
3,4,5,6-tetrahydro-2'-dUMP
-
high-affinity inhibitor, rapid, reversible inhibition, kinetics of inhibition. At low substrate or competitor concentrations: activation. Tetrahydro-dUMP activates enzyme at low substrate concentrations
5-hydroxymethyl-dCTP
-
-
5-hydroxymethyl-dCTP
-
natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP; pH-dependent activation
5-hydroxymethyl-dCTP
-
natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP; pH-dependent activation
5-hydroxymethyl-dCTP
-
30% activation
5-hydroxymethyl-dCTP
-
natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP
5-hydroxymethyl-dCTP
-
natural activator, required for activity; natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP
5-hydroxymethyl-dCTP
-
natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP
5-hydroxymethyl-dCTP
-
natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP
ammonium sulfate
-
substrate dCMP-Hg-S-CH2-CH2-OH, 0.2 M ammonium sulfate: activation, reversed by cCTP
CDP
-
low activation, allosteric activator
CTP
-
low activation, allosteric activator
CTP
-
no activation
dAMP
-
competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate, dAMP activates dCMPase 4fold at low substrate concentration, no activating effect on the modified enzyme, glutaraldehyde-dCMPase
dAMP
-
0.025 mM: low activation
dAMP
-
at low substrate, dCMP, concentration: activation at higher concentration of either: inhibition
dCDP
-
low activation, allosteric activator
dCDP
-
100% activation
dCMP
-
allosterically increases dCMPD activity
dCTP
-
activation, absolute requirement for dCTP
dCTP
-
activate form: dCTP-enzyme; allosteric activator; dCMPase is activated 15.3fold, glutaraldehyde-dCMPase only 1.8fold; glutaraldehyde fixes dCMPase in the activated conformation induced by dCTP
dCTP
-
activation by dCTP has absolute requirement for the presence of a divalent cation, Mg2+, Ca2+ and Mn2+ are equally effective cations for enzyme activation by dCTP; allosteric activator; less than 0.001 mM: very high activation
dCTP
-
severalfold activation, activation requires presence of Mg2+
dCTP
-
allosteric activator; allosteric activator, increases substrate affinity
dCTP
-
allosteric activator; allosteric activator, 12fold, for aminohydrolysis of dCMP, inhibitor, 50% inhibition, for substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH
dCTP
-
positive allosteric effector
dCTP
-
dCTP not required and not activared by dCTP
dCTP
-
required, enzyme requires dCTP, Zn2+, and 2-mercaptoethanol
dCTP
bacteriophage SP8
-
dCTP not required and not activared by dCTP
dCTP
Cricetinae, Herpes simplex virus
-
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
dCTP
-
maximum activation at 0.04 mM, dCTP activation requires presence of Mg2+ or Mn2+; positive allosteric effector
dCTP
-
positive allosteric effector
dCTP
-
activation by dCTP decreases markedly as the pH is increased, pH-dependent activation; positive allosteric effector
dCTP
-
pH-dependent activation; positive allosteric effector
dCTP
-
positive allosteric effector; specifically markedly activated, Km: 0.00017 mM
dCTP
-
positive allosteric effector
dCTP
-
positive allosteric effector; severalfold activation, activation requires presence of Mg2+
dCTP
-
hexameric form of enzyme is activated by dCTP, while the dimer is not; mutants R115E and R115Q: dCTP not required. R115Q: slight, 30-40% activation by 0.02 mM dCTP; positive allosteric effector; required for activity; severalfold activation, activation requires presence of Mg2+; wild-type, dCTP required for activity, no activity in absence of dCTP and Mg2+
dCTP
-
positive allosteric effector; severalfold activation, activation requires presence of Mg2+
dCTP
-
mutant F112A, dCTP not required; positive allosteric effector; wild-type, dCTP required for activity, no activity in absence of dCTP and Mg2+
dCTP
-
positive allosteric effector
dCTP
-
activation by dCTP is reversed by addition of dTTP; allosteric activator; positive allosteric effector
dCTP
-
dCTP promotes an aggregation of enzyme subunits to the active state; positive allosteric effector
dCTP
-
positive allosteric effector
dCTP
-
positive allosteric effector
dCTP
-
positive allosteric effector
dCTP
-
activation by dCTP is reversed by addition of dTTP; dCTP promotes an aggregation of enzyme subunits to the active state; positive allosteric effector
dCTP
Herpes simplex virus
-
-
dCTP
-
activation by dCTP is reversed by addition of dTTP; positive allosteric effector
dCTP
-
positive allosteric effector
dCTP
-
an allosteric activator, in complex with Mg2+
dCTP
O41078, -
activates dCMP deamination about 7fold at 0.005-0.1 mM
deoxycytidine 5'-triphosphate
-
allosteric feedback regulation of the enzyme by products of the metabolic pathway, allosteric regulation involved residues 112 and 115
dGTP
-
very slight activation
dTTP
-
allosteric inhibitor, 100% inhibition, for substrate dCMP, becomes activator, 2.5fold, for mercury substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH, at relatively high, 1 to 2 mM, dCMP-Hg-S-CH2-CH2-OH concentration
dTTP
-
no activation
dTTP
-
allosteric inhibitor, 100% inhibition, for substrate dCMP, becomes activator, 2.5fold, for mercury substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH, at relatively high, 1 to 2 mM, dCMP-Hg-S-CH2-CH2-OH concentration
dUTP
-
89% activation
Glutaraldehyde
-
substrate dCMP: rapid inhibition, protection by dGMP, or dTTP or both is slight, substrate dCMP-Hg-S-CH2-CH2-OH: 3fold activation
glycerol
-
substrate dCMP: activation, substrate dCMP-Hg-S-CH2-CH2-OH, 20% glycerol: inhibition
pre-immune serum
-
activation of host-cell enzyme, twice as effective as Herpes antiserum
-
TTP
-
activating enzyme up to 1.7fold at concentration of 0.00025 mM, but inhibiting at higher concentration, 0.015 mM: 85% inhibition
Herpes antiserum
-
activation of host-cell enzyme
-
additional information
-
no activation by ATP, UTP, CTP and dTTP
-
additional information
Cricetinae, Herpes simplex virus
-
no activation by KCl up to 0.3 M
-
additional information
-
mechanism of activation
-
additional information
-
the phage dCMP deaminase expression is increased upon infection of Escherichia coli
-
additional information
-
no activation by deoxynucleotide triphosphates
-
additional information
-
infection with the human cytomegalovirus upregulates the enzyme involved in thymidylate synthesis especially the dCMP deaminase, but not the dUTPase, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
5-methyl-dCMP
-
pH 8.3, in the presence of dCTP or 5-hydroxymethyl-dCTP. Decreasing the pH to 6.0 lowers the apparent Km
10
-
CMP
-
pH 8.3, in the presence of dCTP or 5-hydroxymethyl-dCTP. Decreasing the pH to 6.0 lowers the apparent Km
12
-
CMP
-
pH 8.0, absence of effector
0.021
-
dCMP
-
recombinant wild-type enzyme, pH 8.0, 30C; wild-type, presence of dCTP and Mg2+
0.022
-
dCMP
-
pH 7.5
0.024
-
dCMP
-
in the presence of dCTP
0.037
-
dCMP
-
in the presence of dCTP
0.05
-
dCMP
-
pH 6.0
0.1
-
dCMP
-
pH 8.3, in the presence of dCTP or 5-hydroxymethyl-dCTP. Decreasing the pH to 6.0 lowers the apparent Km
0.127
-
dCMP
-
R115Q, absence of dCTP; recombinant mutant R115Q, pH 8.0, 30C
0.137
-
dCMP
-
R115E, absence of dCTP; recombinant mutant R115E, pH 8.0, 30C
0.32
-
dCMP
Cricetinae, Herpes simplex virus
-
in the presence of dCTP and presence of 2 mM Mg2+
0.76
-
dCMP
O41078, -
pH 9.5, 42C, in presence of 0.1 mM dCTP
0.91
-
dCMP
Cricetinae, Herpes simplex virus
-
in the presence of dCTP and absence of 2 mM Mg2+
0.91
-
dCMP
-
-
0.26
-
dCMP-Hg-S-CH2-CH2-OH
-
-
-
0.64
-
dCTP
O41078, -
pH 9.5, 42C
0.347
-
Deoxycytidine
-
pH 8.1, 37C, Rat-2 fibroblasts in presence of 0.02 mM docosahexanoic acid
0.349
-
Deoxycytidine
-
pH 8.1, 37C, Rat-2 fibroblasts
0.462
-
Deoxycytidine
-
pH 8.1, 37C, NM-16 fibroblasts
0.467
-
Deoxycytidine
-
pH 8.1, 37C, NM-16 fibroblasts in presence of 0.02 mM docosahexanoic acid
additional information
-
additional information
-
preliminary kinetic studies and kinetic data
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data, kinetics typical of activated enzyme; kinetic experiments; Km-value of modified enzyme, glutaraldehyde-dCMPase, is lower than that of native enzyme
-
additional information
-
additional information
-
kinetic behavior and data
-
additional information
-
additional information
-
preliminary kinetic studies and kinetic data
-
additional information
-
additional information
-
kinetic studies, steady-state kinetics, allosteric kinetics
-
additional information
-
additional information
-
kinetic experiments; kinetic properties and parameters
-
additional information
-
additional information
-
kinetic properties and parameters
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
cooperative kinetics, kinetic affinities and effects, mechanism
-
additional information
-
additional information
-
cooperative kinetics, kinetic affinities and effects, mechanism; steady-state kinetic Hill coefficients, allosteric enzyme kinetic data
-
additional information
-
additional information
-
kinetics of inhibition
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic analysis, data and characterization of wild-type and mutants R115E, R115Q and F112A
-
additional information
-
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
24.9
-
dCMP
O41078, -
pH 9.5, 42C, in presence of 0.1 mM dCTP
69
-
dCMP
-
mutant R115E, pH 8.0, 30C; R115E
85
-
dCMP
-
mutant R115Q, pH 8.0, 30C; R115Q dimer
255
-
dCMP
-
R115Q hexamer
466
-
dCMP
-
wild-type; wild-type enzyme, pH 8.0, 30C
960
-
dCMP
-
-
1400
-
dCMP
-
-
5.7
-
dCTP
O41078, -
pH 9.5, 42C
additional information
-
additional information
-
mutants R115E and R115Q possessing turnover number or kcat that is about 15% that of wild-type enzyme
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0394
-
2',3'-dihydro-2',3'-dideoxy-thymidine monophosphate
-
pH 7.5
0.0367
-
3'-azido-2',3'-dideoxy-thymidine monophosphate
-
pH 7.5
0.0142
-
5-fluoro-dUMP
-
pH 7.5
0.0103
-
D-beta-2'-fluoro-5-methyl-arabinofuranosyluracil monophosphate
-
pH 7.5
0.0257
-
dUMP
-
pH 7.5
0.0046
-
TMP
-
pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.37
-
-
-
10
-
-
-
23
-
-
substrate: dCMP-Hg-S-CH2-CH2-OH
90
100
-
mutant R115E
121
-
-
mutant R115Q
220
-
-
wild-type
481
-
-
-
500
-
-
HeLa cells
720
-
-
-
730
-
-
-
820
-
-
substrate: dCMP
additional information
-
-
-
additional information
-
-
mutants R115E and R115Q possessing specific activity about 40-50% of wild-type enzyme
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
-
in the absence of dCTP
6.5
7.3
-
broad pH optimum
7
-
O41078, -
dCTP deaminase activity
7.2
-
-
assay at
7.5
8.5
-
HeLa cells, in presence or absence of dCTP and Mg2+
7.5
9.5
-
broad pH optimum
7.5
-
-
assay at
7.5
-
-
assay at
7.8
-
-
assay at
7.8
-
-
pH optimum around
8
-
-
assay at, substrate: dCMP-Hg-S-CH2-CH2-OH
8
-
-
assay at
8
-
-
assay at
8.1
-
-
assay at
8.2
-
-
assay at
8.3
-
-
in the presence of dCTP or 5-hydroxymethyl-dCTP
8.4
-
-
BHK-21/C13 cells
9.5
-
O41078, -
dCMP deaminase activity
additional information
-
-
pI: 5.10
additional information
-
Cricetinae, Herpes simplex virus
-
enzyme from host-cell and Herpes virus-induced enzyme have a similar pH-optimum
additional information
-
-
dCTP increases pH-optimum by approximately 3 pH units
additional information
-
-
dCTP increases pH-optimum by approximately 0.6 unit
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
11
O41078, -
activity range
7
8.5
-
50% maximal activity at pH 7.0 and 8.5
7
9
-
pH 7.0: 60%, pH 8.2: 98% and pH 9.0 96% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
optimum condition
30
-
-
optimum condition
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
Cricetinae, Herpes simplex virus
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
38
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
baby-hamster kidney
Manually annotated by BRENDA team
Sea urchin
-
-
Manually annotated by BRENDA team
-
the enzyme activity is higher in normal Rat-2 fibroblast compared to transformed NM-16 cells
Manually annotated by BRENDA team
-
quiescent cells infected with human cytomegalovirus, HCMV
Manually annotated by BRENDA team
-
BHK-21/C13 cells, baby-hamster kidney cells
Manually annotated by BRENDA team
-
transformed fibroblast cell line
Manually annotated by BRENDA team
-
fibroblast cell line
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
38200
113000
-
recombinant mutant F112A, gel filtration, dependent on protein concentration, in presence and absence of fdCTP
39800
118000
-
recombinant mutant R115Q, gel filtration, dependent on protein concentration, in presence and absence of fdCTP
41600
45400
-
recombinant mutant R115E, gel filtration, dependent on protein concentration, in presence and absence of fdCTP
44300
-
-
R115E, HPLC gel filtration
109500
-
-
gel filtration
110000
122000
-
recombinant wild-type enzyme, gel filtration, dependent on protein concentration, in presence and absence of fdCTP
111900
-
-
F112A, HPLC gel filtration
113100
-
-
amino acid analysis
115000
-
-
BHK-21/C13 cells, sucrose density gradient centrifugation
117000
-
-
in the presence of dCTP and Mg2+, 4C, gel filtration
120000
-
-
PAGE
120000
-
-
-
124000
-
-
PAGE and sedimentation equilibrium
124500
-
-
R115Q, HPLC gel filtration
127000
-
-
wild-type, HPLC gel filtration
130000
-
-
BHK-21/C13 cells, gel filtration
170000
-
-
gel filtration and sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 21200, mutant R115E: dimer, mutants R115Q and F112A varies from hexamers to dimers or something in between depending on protein concentration, HPLC gel filtration in the presence of SDS; mutants R115Q and R115E, mutant F112A changes between dimeric and hexameric forms
dimer
-
the mutant R115E is dimeric in solution, while hexameric in crystals, quarternary structure analysis
hexamer
-
6 * 20000, SDS-PAGE; 6 identical subunits
hexamer
-
6 * 20200, sedimentation in 6 M guanidine hydrochloride containing 0.1 M 2-mercaptoethanol and SDS-PAGE; 6 identical subunits; hexamer is the active form
hexamer
-
6 * 18842, amino acid analysis; 6 identical subunits
hexamer
-
6 * 21200, wild-type, particularly in the presence of dCTP: hexamer, mutants R115Q and F112A varies from hexamers to dimers or something in between depending on protein concentration, HPLC gel filtration in the presence of SDS; 6 identical subunits; wild-type enzyme, mutant F112A changes between dimeric and hexameric forms
hexamer
-
6 identical subunits
hexamer
-
6 * 20000, HeLa cells, SDS-PAGE and amino acid sequence; 6 * 20000, SDS-PAGE; 6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
6 * 20000, HeLa cells, SDS-PAGE and amino acid sequence; 6 identical subunits
hexamer
-
6 identical subunits
hexamer
-
homohexamer, subunits adopt a three-layer alpha/beta/alpha sandwich fold
hexamer
O41078, -
6 * 17000, SDS-PAGE
additional information
-
hexameric form of enzyme is activated by dCTP, while the dimer is not
additional information
-
monomeric and quarternary structure analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified mutant R115E free or in complex with active site binding inhibitor pyrimidin-2-one deoxyribotide, the mutant R115E is dimeric in solution, while hexameric in crystals, hanging drop vapour diffusion method, 0.28 mM mutant R115E protein in 20 mM phosphate, pH 7.2, 0.38 mM inhibitor, and 30 mM DTT, is mixed with an equal volume of reservoir solution containing 1.3 M ammonium sulfate, 0.1 M sodium citrate, pH 6.0, and 10 mM DTT, 22C, 3 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
dCMP deaminase in complex with dCTP and an intermediate analogue, X-ray diffraction structure determination and analysis at 1.66-3.0 A resolution, the crystal structure of the free-state enzyme is determined by the zinc multiwavelength anomalous dispersion, MAD, method
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
half-life: 30 min, Zn2+, thiols, 2-mercaptoethanol, and dCTP protect against inactivation
37
-
Cricetinae, Herpes simplex virus
-
enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster is more resistant to heating at 37C than enzyme from non-infected cells. In the presence of 0.125 mM dCTP and 2 mM Mg2+, 100% stable, 20 min at 37C
43
-
-
in the presence of ethyleneglycol: 100% stable
50
-
-
thiol, 2-mercaptoethanol, dCTP and Zn2+ protect the enzyme against heat inactivation at 50C
50
-
-
ethyleneglycol stabilizes against thermal inactivation, when temperature increases to 50C, leads to certain increase in specific activity
50
-
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and Mg2+, or by increasing protein concentration
additional information
-
-
dCTP, and to a lesser extent dTTP, stabilizes against heat inactivation
additional information
-
-
ethyleneglycol stabilizes against thermal and UV inactivation
additional information
-
Cricetinae, Herpes simplex virus
-
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
additional information
-
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol stabilizes
-
thiols stabilize
-
thiols, such as 2-mercaptoethanol or dithiothreitol, stabilize, in the absence of thiols the enzyme is highly unstable
-
Zn2+ or dCTP stabilize, protect against inactivation
-
dCTP and Mg2+ stabilize
-
dCTP, 0.125 mM, or ethyleneglycol, 20% v/v, stabilize
-
enzyme very heat-labile, stabilized against heat inactivation by dCTP, 0.125 mM and ethyleneglycol, 20% v/v
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
-
2-mercaptoethanol stabilizes
-
dCTP stabilizes
-
dCTP stabilizing hexameric state, dTTP destabilizing
-
dCTP, or to a lesser extent dTTP, stabilize against heat inactivation, protein denaturants and proteolytic enzymes
-
guanidine hydrochloride, 1 M, complete loss in activity accompanied by disaggregation of enzyme, 6 M: denaturation, complete reactivation with 50 mM 2-mercaptoethanol
-
thiols stabilize
-
2-mercaptoethanol stabilizes
-
dCTP stabilizes
-
EDTA: denaturation, EDTA removes the two resident Zn2+ atoms /subunit
-
guanidine-HCl, 6 M, denaturation, complete restoration of activity on removal of denaturant by dilution or dialysis
-
dCTP or glycerol stabilize
-
dCTP stabilizing hexameric state, dTTP destabilizing
-
glycerol stabilizes
-
dCTP stabilizes
-
enzyme is unstable
-
enzyme very sensitive to preliminary heating, dCTP, 0.125 mM, and Mg2+, 2 mM, stabilize against heat inactivation
Herpes simplex virus
-
2-mercaptoethanol stabilizes
-
dCTP and MgCl2 stabilize
-
dithiothreitol, 2 mM, stabilizes
-
enzyme extremely labile, stabilized by dCTP /Mg2+
-
ethyleneglycol prevents protein denaturation during freezing in the presence of 2-mercaptoethanol
-
ethyleneglycol, 10-20% stabilizes
-
glycerol, 15%, stabilizes
-
enzyme is unstable
-
2-mercaptoethanol stabilizes
-
dCTP or glycerol stabilize
-
ethyleneglycol, 20%, stabilizes against thermal and UV inactivation and denaturation factors with different mechanism of action
-
glycerol stabilizes
-
some free nucleotides, most effective dCTP, stabilize
-
highly stable enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, pH 7.8, 2 mM 2-mercaptoethanol
-
0C, 2-mercaptoethanol, stable for more than 6 h
-
0C, half-life: 30 min
-
-70C, 20% v/v ethyleneglycol, stable for 2 months
-
0-4C, neutral pH, 0.1 M 2-mercaptoethanol, stable for several months
-
frozen in absence of 2-mercaptoethanol, indefinitely stable
-
-40C, solid ammonium sulfate to 80% saturation, stable for longer periods of storage
-
0-4C, 0.1 M 2-mercaptoethanol, stable for extended periods
-
-20C, 0.1 M Na-phosphate, pH 7.5, 50% glycerol, 12 months, no activity lost
-
-20C, 10-20% ethyleneglycol, 0.01 mM dCTP, 1 mM MgCl2, 20 mM 2-mercaptoethanol and 0.05% Triton X-100, 1 year, no loss in activity
-
-50C, 0.05 mM dCTP, 1 mM MgCl2 or 2 mM dithiothreitol, 18 h, 40% activity lost
-
on ice, 0.05 M Tris, pH 8.0, 20 mM dithiothreitol, stable for weeks
-
the purified recombinant His-tagged enzyme in stable without precipitation for more than 1 year in 50% glycerol
O41078, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
BHK-21/C13 cells , enzyme from non-infected cells and cells infected by Herpes simplex
-
partial, BHK-21/C13 cells, baby-hamster
-
T2-phage infected Escherichia coli
-
cloned wild-type and mutant F112A
-
recombinant mutant R115E from Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli; wild-type and mutants R115E, R115Q and F112A
-
T4-phage infected Escherichia coli
-
host baby-hamster, BHK-21/C13 cells
Herpes simplex virus
-
HeLa cells
-
native enzyme 60fold from Hep-G2 cells by adsorption chromatography
-
native enzyme from sperm cells by ion exchange chromatography and preparative SDS-PAGE
-
partial, leukemia cells
-
partial, Ehrlich's ascites tumor cells
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, the protein quickly precipitates at concentration higher than 2 mg/ml
O41078, -
partial, strain ACM-13
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned and amplified in a high-expression system, expression in Escherichia coli strain BL21-DE3/pLysS
-
expression of mutant R115E in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
cDNA from HeLa cells can be expressed in an active form
-
cloned and overexpressed in Escherichia coli strain BL21-DE3/pLysS
-
ORF A596R, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain DH5MCR, phylogenetic analysis
O41078, -
overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F112A
-
molecular weight analysis using HPLC gel filtration in the presence of SDS and dCTP: wild-type is a hexamer, F112A varies from hexamer to dimer; site-directed mutagenesis, the mutant enzyme shows reduced turnover and activity compared to the wild-type enzyme
F112A
-
as active as wild-type even in the absence of dCTP and only weakly inhibited by dTTP, loss of allosteric regulation by dCTP and dTTP, no activation by dCTP, no inhibition by dTTP
R115E
-
mutant enzyme active in the absence of dCTP and Mg2+, little if any activation by dCTP, possessing turnover number or kcat that is about 15% that of wild-type enzyme, specific activity about 40-50% of wild-type enzyme. Molecular weight analysis using HPLC gel filtration in the presence of SDS and dCTP: wild-type is a hexamer, R115E a dimer; site-directed mutagenesis, the mutant enzyme shows reduced turnover and activity compared to the wild-type enzyme, but no longer requires deoxycytidine 5-triphosphate for activation in contrast to the wild-type enzyme
R115E
-
site-directed mutagenesis, quarternary structure analysis
S178F
-
site-directed mutagenesis, the mutation is responsible for MNNG resistance in the drm1-1 strain,
R115Q
-
mutant enzyme active in the absence of dCTP and Mg2+, possessing turnover number or kcat that is about 15% that of wild-type enzyme, specific activity about 40-50% of wild-type enzyme. Molecular weight analysis using HPLC size gel filtration in the presence of SDS and dCTP: wild-type is a hexamer, R115Q varies from hexamer to dimer; site-directed mutagenesis, the mutant enzyme shows reduced turnover and activity compared to the wild-type enzyme, but no longer requires deoxycytidine 5-triphosphate for activation in contrast to the wild-type enzyme
additional information
-
construction of a dcd1DELTA enzyme-deficient strain, the deletion strain and the dcd1-S178F mutant strain are crossed with a rad52DELTA mgt1DELTA strain and haploid, double and triple mutant strains are generated, rad52DELTA mgt1DELTA dcd1-S178F and rad52DELTA mgt1DELTA dcd1DELTA strains show an increased level of MNNG resistance, while the only dcd1-deficient strain does not, overview, DCD1 deficiency in yeast results in elevation of dCTP pools and a slight decrease in dTTP pools and reduced the frequency of spontaneous and MNNGinduced G/C to A/T mutations, phenotypes, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after treatment with guanidine hydrochloride, 6 M, complete reactivation with 50 mM 2-mercaptoethanol, original hexameric structure restored
-
after denaturation with EDTA, mutants R115E and R115Q restored 54% and 60% of original activities, wild-type enzyme only marginally restored; after treatment with guanidine-HCl, 6 M, complete reactivation on removal of denaturant by dilution or dialysis
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
the enzyme is a major target for cancer chemotherapy
pharmacology
-
might have applications in cancer chemotherapy. Enzyme may be an inhibitor target for antitumor agents
medicine
-
associated mainly with dividing tissues, potential diagnostic tool for various disease states in which enzyme is elevated
pharmacology
-
elevated level of dCMPase in transformed cells and tumors: enzyme may represent another important target for cancer chemotherapy
pharmacology
-
enzyme might be a reasonable target for chemotherapeutic agents directed against parasitic as well as neoplastic diseases by limiting the synthesis of dUMP, particularly when used in combination with inhibitors of dTMP synthase or other purine and pyrimidine inhibitors of DNA synthesis