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Information on EC 3.5.4.5 - cytidine deaminase and Organism(s) Homo sapiens and UniProt Accession P32320

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.5 cytidine deaminase
IUBMB Comments
Contains zinc. Catalyses the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
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Homo sapiens
UNIPROT: P32320
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
cytidine deaminase, activation-induced cytidine deaminase, aicda, deoxycytidine deaminase, cr deaminase, cyd deaminase, t-cda, cytosine nucleoside deaminase, cytidine aminohydrolase, yeast cytidine deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
activation-induced cytidine deaminase
-
-
-
-
AICDA
-
-
-
-
CR deaminase
-
-
cyd deaminase
-
-
Cytidine aminohydrolase
-
-
-
-
cytidine deaminase
-
-
cytidine/2'-deoxycytidine aminohydrolase
-
-
cytosine nucleoside deaminase
-
-
-
-
DCD
-
-
-
-
T-CDA
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
amidine hydrolysis
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
cytidine/2'-deoxycytidine aminohydrolase
Contains zinc. Catalyses the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
CAS REGISTRY NUMBER
COMMENTARY hide
37259-56-6
-
9025-06-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
2',2'-difluorodeoxycytidine + H2O
2',2'-difluorodeoxyuridine + NH3
show the reaction diagram
2',3'-dideoxycytidine + H2O
2',3'-dideoxyuridinel + NH3
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-fluoro-2'-deoxy-5-iodocytosine arabinoside + H2O
?
show the reaction diagram
-
-
-
-
?
2'-fluoro-2'-deoxycytidine + H2O
2'-fluoro-2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
3'-amino-2',3'-dideoxycytidine + H2O
3'-amino-2',3'-dideoxyuridine + NH3
show the reaction diagram
-
-
-
?
5'-chlorocyclocytidine + H2O
5'-chlorocyclouridine + NH3
show the reaction diagram
-
i.e. cytosine, 1beta-D-arabinofuranosyl-2,2'-anhydro-, hydrochloride
-
-
?
5'-deoxyfluorocytidine + H2O
5'-deoxy-5-fluorouridine + NH3
show the reaction diagram
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-aza-2'-deoxycytidine + H2O
5-aza-2'-deoxyuridine + NH3
show the reaction diagram
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
?
5-azadeoxycytidine + H2O
5-azadeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-bromocytidine + H2O
5-bromouridine + NH3
show the reaction diagram
-
-
-
-
?
5-chlorocytidine + H2O
? + NH3
show the reaction diagram
-
-
-
-
?
5-iodo-2'-deoxycytidine
5-iodo-2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-iodocytidine + H2O
5-iodouridine + NH3
show the reaction diagram
-
-
-
-
?
5-iododeoxycytidine + H2O
5-iododeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
-
-
-
-
?
6-azacytidine + H2O
6-azauridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
cytosine arabinoside + H2O
?
show the reaction diagram
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
gemcitabine + H2O
2'-deoxy-2',2'-difluorouridine
show the reaction diagram
-
CDA is the major enzyme involved in gemcitabine inactivation, a cytotoxic drug commonly used in the treatment of pancreas and non-small cell lung cancer
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-aza-2'-deoxycytidine + H2O
5-aza-2'-deoxyuridine + NH3
show the reaction diagram
-
5-AZA-CdR shows an antineoplastic action on 3T3 cells and V5 cells transduced with CR deaminase gene, pharmakokinetic analysis in mice, overview
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
cytosine arabinoside + H2O
?
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
additional information
?
-
-
cytidine deaminase plays an important role in the activation of the anticancer drug capesitabine in the human body
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(cytidyl)acryloylaminohexanoic acid
-
i.e. CV6
1,10-phenanthroline
-
-
1-(beta-D-ribofuranosyl)-dihydropyrimidine-2-one
2'-deoxyuridine
-
-
2'-deoxyzebularine 5'-monophosphate
-
-
2-thio-6-azarudine
-
-
3'-azido-3'-deoxythymidine
-
-
3,4,5,6-Tetrahydrouridine
3-deazauridine
4-amino-1-(5-hydroxypentyl)pyrimidin-2(1H)-one
-
-
4-amino-1-hexyl-5,6-dihydropyrimidin-2(1H)-one
-
-
4-hydroxy-1-(beta-D-ribofuranosyl)piperidin-2-one
-
-
5,6-Dihydrouridine
-
-
5-(Chloromercuri)cytidine
-
-
5-Bromouridine
-
-
5-fluoro-2'-deoxyuridine
5-fluorouridine
-
-
5-fluorozebularine
-
-
5-iodo-2'-deoxyuridine
-
-
5-methyluridine
-
-
5-{(1E)-3-[(5-carboxypentyl)amino]-3-oxoprop-1-en-1-yl}-5,6-dihydrocytidine
6-azauridine
-
-
6-[3-(5-cytidyl)acryloylamino]hexanoic acid
-
i.e. CV6
ara-U
-
-
cytidine monophosphate
-
-
deoxyadenosine
-
-
diazepinone riboside
dipicolinic acid
-
-
DTNB
-
-
dTTP
-
-
N-ethylmaleimide
p-chloromercuribenzoate
-
-
pseudouridine
-
-
SDS
-
wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated monomers restores completely the activity. 5-Fluorozebularine disfavours dissociation of the tetramer into subunits in the wild-type enzyme, but not in the mutant enzyme F137W/W113F
tetrahydrouridine
-
THU, the presence of 1 microM totally prevents the formation of 5'-deoxy-5-fluorouridine in blood samples of healthy volunteers and capecitabine-treated patients
thymidine
-
-
thymine riboside
uridine
zebularine
-
inhibits the enzyme, but also DNA methylation, competitive versus 5-aza-2'-deoxycytidine, zebularine affects the antineoplastic action of 5-AZA-CdR on 3T3 cells and V5 cells transduced with CR deaminase gene, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 2.8
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine
0.33
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
-
-
0.27
1-beta-D-arabinofuranosylcytosine
-
-
0.0092 - 0.0957
2',2'-difluorodeoxycytidine
0.0726
2',2'-difluorodeoxyuridine
-
i.e. dFdU, variation of plasma ranges between 24.9 and 72.6 microM
0.023 - 0.4
2'-deoxycytidine
0.0477
5-aza-2'-deoxycytidine
-
pH 7.4, 37°C
0.058 - 0.31
5-azacytidine
0.087 - 0.1
5-iododeoxycytidine
0.04
5-methylcytidine
-
recombinant CDA
4.2
6-azacytidine
-
-
0.0092 - 0.27
cytidine
0.11 - 0.385
cytosine arabinoside
0.039 - 0.055
deoxycytidine
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 0.045
(cytidyl)acryloylaminohexanoic acid
0.00042 - 0.008
3,4,5,6-Tetrahydrouridine
0.015 - 0.04
5,6-Dihydrouridine
0.00006 - 0.0017
5-fluorozebularine
0.015 - 0.045
6-[3-(5-cytidyl)acryloylamino]hexanoic acid
0.3 - 0.39
cytidine monophosphate
0.000025
diazepinone riboside
-
-
0.1 - 0.4
uridine
0.00095
zebularine
-
pH 7.4, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00164
-
-
0.0059
-
-
0.011
-
-
0.536
-
activity in non-small cell lung cancer patients with CDA Lys27Lys protein, in 50 mM beta-mercaptoethanol, 0.1 M Tris-HCl, pH 8.0, substrate 0.25 mM gemcitabine
0.7254
-
activity in non-small cell lung cancer patients carrying the Lys27Gln polymorphism and the Gln27Gln polymorphism, in 50 mM beta-mercaptoethanol, 0.1 M Tris-HCl, pH 8.0, substrate 0.25 mM gemcitabine
29
-
colon tumour
3.96
-
sarcoma tumour
64.1
-
-
738
-
ovarian tumour
86.7
-
pancreas tumour
additional information
-
variation between 1.51 to 5.50 nmol/h/mg protein, about 100-fold lower than that in liver
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 10.5
-
deoxycytidine as substrate, beyond these values irreversible inactivation occurs
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 62
-
mutant Y60G shows an unusual behavior with a mean of 75% activity for temperatures within this range and three peaks of maximum activity at about 30°C, 46°C, and 62°C
37
-
assay at
58
-
recombinant wild-type enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 65
-
mutant Y60G shows an unusual behavior with a mean of 75% activity for temperatures within this range and three peaks of maximum activity at about 30°C, 46°C, and 62°C
37 - 75
-
60% of maximal activity at 75°C for the wild-type enzyme, 35% for mutant R68Q
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
tetramer of recombinant subunit CDA2, isoelectric focusing
4.55 - 4.9
-
5 different isoforms of native enzyme, isoelectric focusing
5
-
tetramer of recombinant subunit CDA1, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression level
Manually annotated by BRENDA team
-
glioblastoma multiforme (GBM) patients
Manually annotated by BRENDA team
-
glioblastoma multiforme (GBM) patients
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CDA enables toll-like receptor TLR8 activation by cytidine or its analogues with ssRNA through deaminating activity. CDA expression enables TLR8 response to cytidine and ssRNA in 293T cells. CDA deficiency and a CDA inhibitor both reduces TLR8 responses to cytidine and ssRNA in U937. The CDA inhibitor also reduces peripheral blood leukocyte response to cytidine and ssRNA. Analogue azacytidine with ssRNA induces tumor necrosis factor-alpha expression in U937 and peripheral blood leukocytes in a manner dependent on CDA and TLR8
evolution
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CDD_HUMAN
146
0
16185
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13500
-
4 * 13500, SDS-PAGE
15000
16000
-
estimated from cDNA open reading frame coding for human cytidine deaminase
16170
-
deduced from cDNA nucleotide sequence
51000
-
human granulocytes
52000
-
gel filtration
57000
-
gel filtration
60000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
-
wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated mponomers restores completely the activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of theoretically predicited model and experimentally elucidated structure
-
in complex with inhibitor diazepinone riboside. Inhibitor is able to establish a canonical pi/pi interaction with key active site residue F137
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F137A
-
site-directed mutagenesis, inactive monomeric enzyme
F137W/W113F
-
5-fluorozebularine does not protect mutant enzyme from dissociation by SDS as it does protect the wild-type enzyme
R68G
-
site-directed mutagenesis, the mutant R68G shows reduced activity compared to the wild-type enzyme and dissociates very easily in presence of small amounts of SDS
R68Q
-
site-directed mutagenesis, the mutant shows reduced activity and thermal stability compared to the wild-type enzyme, but the quaternary structure of R68Q is not affected by the mutation
Y33F
-
site-directed mutagenesis, inactive monomeric enzyme
Y33G
-
site-directed mutagenesis, inactive monomeric enzyme
Y33S
-
site-directed mutagenesis, inactive monomeric enzyme
Y60G
-
site-directed mutagenesis, the mutant shows a more compact quaternary structure with respect to the wild-type enzyme, and a slightly reduced activity as well as altered thermal stability
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 10.5
-
deoxycytidine as substrate, beyond these extremes rapid inactivation
209661
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 75
-
wild-type enzyme and mutant R68Q are stable, while the stability of mutant Y60G is decreased above 65°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris-HCl, pH 7.5, 1 mM DDT, 1 mM EDTA, 20% glycerol, enzyme retains full activity for at least 1 month, 80% of activity lost in absence of glycerol
-
-20°C, 20% glycerol appears to be necessary to prevent inactivation from occuring after freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme partially from 3T3 NIH and 3T3-CD3-V5 cells by ammonium sulfate fractionation
-
recombinant wild-type enzyme by affinity chromatography on a cytidine analog 6-[3,5(cytidyl) acryloylamino]hexanoic acid resin, recombinant inactive mutants by anion exchange chromatography, ultrafiltration, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, PCR, vector pTrc99A, cloned and expressed in Escherichia coli DH5alpha
-
expression of wild-type and mutant enzymes in Escherichia coli, complementation of enzyme enzyme-deficient strain by the wild-type enzyme and mutants Y60G, R68Q, and R68G, not by F33 and F137A mutants
-
functional expression of the human enzyme in murine fibroblast cell lines 3T3 NIH and 3T3-CD3-V5 cells, and in the murine lymphocytic leukemia cell line L1210
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of DMSO (3-7% final concentrations) or glycerol (5-10% final concentrations) to the culture medium increases the expression of the mutant enzyme Y33G
-
sorbitol or cyclodextrins does not induce expression of the mutant enzyme Y33G
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
cytidine deaminase as prognostic marker in non-small-cell lung cancer. In the patients with high versus low CDA activity the response rate is 25.0% and 54.1%, the 6-month progression rate is 34.5% and 54.1%, the 1-year survival rate is 23.3% and 57.3%, respectively
diagnostics
-
evaluation of CDA genotype may be helpful in screening patients before treatment, in order to identify subjects with slower CDA-mediated gemcitabine metabolism
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jahns-Streubel, G.; Unterhalt, M.; Schleyer, E.; Reuter, C.; Wrmann, B.; Buchner, T.; Hiddemann, W.
Correlation of deoxycytidine deaminase, thymidine kinase and polymerase alpha activity and deoxycytidine deaminase gene expression in vivo with clinical response to TAD-9+GM-CSF induction therapy in acute myeloid leukemia
Haematol. Blood Transfus.
38
252-259
1997
Homo sapiens
-
Manually annotated by BRENDA team
Mancini, W.R.
The role of deoxycytidine-metabolizing enzymes in the cytotoxicity induced by 3'-amino-2',3'-dideoxycytidine and cytosine arabinoside
Cancer Chemother. Pharmacol.
30
139-144
1992
Homo sapiens
Manually annotated by BRENDA team
Ruiz van Haperen, V.W.T.; Veerman, G.; Braakhuis, B.J.M.; Vermorken, J.B.; Boven, E.; Leyva, A.; Peters, G.J.
Deoxycytidine kinase and deoxycytidine deaminase activities in human tumour xenografts
Eur. J. Cancer
29A
2132-2137
1993
Homo sapiens
Manually annotated by BRENDA team
Kroep, J.R.; van Moorsel, C.J.A.; Veerman, G.; Voorn, D.A.; Schultz, R.M.; Worzalla, J.F.; Tanzer, L.R.; Merriman, R.L.; Pinedo, H.M.; Peters, G.J.
Role of deoxycytidine kinase (dCK), thymidine kinase 2 (TK2), and deoxycytidine deaminase (dCDA) in the antitumour activity of gemcitabine (dFdC)
Adv. Exp. Med. Biol.
431
657-660
1998
Homo sapiens
Manually annotated by BRENDA team
Cohen, R.M.; Wolfenden, R.
Cytidine deaminase from Escherichia coli. Purification, properties and inhibition by the potential transition state analog 3,4,5,6-tetrahydrouridine
J. Biol. Chem.
246
7561-7565
1971
Escherichia coli, Escherichia coli B / ATCC 11303, Homo sapiens, Mus musculus, Mus musculus BALB/c, Ovis aries, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Abell, C.W.; Marchand, N.W.
Cytidine deaminase in human lymphocytes
Nature New Biol.
244
217-219
1973
Homo sapiens
Manually annotated by BRENDA team
Wentworth, D.F.; Wolfenden, R.
On the interaction of 3,4,5,6-tetrahydrouridine with human liver cytidine deaminase
Biochemistry
14
5099-5105
1975
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Wentworth, D.F.; Wolfenden, R.
Cytidine deaminases (from Escherichia coli and human liver)
Methods Enzymol.
51
401-407
1978
Canis lupus familiaris, Cavia porcellus, Columba sp., Escherichia coli, Escherichia coli B / ATCC 11303, Felis catus domesticus, Homo sapiens, Macaca mulatta, Mus musculus, Mus musculus BALB/c, Oryctolagus cuniculus, Rana sp., Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Rothman, I.K.; Malathi, V.G.; Silber, R.
Cytidine deaminase from leukemic mouse spleen
Methods Enzymol.
51
408-412
1978
Homo sapiens, Mus musculus, Mus musculus BALB/c
Manually annotated by BRENDA team
Ashley, G.W.; Bartlett, P.A.
Purification and properties of cytidine deaminase from escherichia coli
J. Biol. Chem.
259
13615-13620
1984
Escherichia coli, Escherichia coli B / ATCC 11303, Homo sapiens, Mus musculus, Mus musculus BALB/c, Ovis aries, Saccharomyces cerevisiae, Zea mays
Manually annotated by BRENDA team
Ashley, G.W.; Bartlett, P.A.
Inhibition of Escherichia coli cytidine deaminase by a phosphopyrimidine nucleoside
J. Biol. Chem.
259
13621-13627
1984
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Fanucchi, M.P.; Watanabe, K.A.; Fox, J.J.; Chou, T.
Kinetics and substrate specificity of human and canine cytidine deaminase
Biochem. Pharmacol.
35
1199-1201
1986
Canis lupus familiaris, Homo sapiens
Manually annotated by BRENDA team
Nygaard, P.
On the role of cytidine deaminase in cellular metabolism
Adv. Exp. Med. Biol.
195B
415-420
1986
Saccharomyces cerevisiae, Escherichia coli, Ovis aries, Homo sapiens, Mus musculus, no activity in Lactobacillus sp., no activity in Moraxella sp., no activity in Pseudomonas sp., Salmonella enterica subsp. enterica serovar Typhimurium, Zea mays, Mus musculus BALB/c
Manually annotated by BRENDA team
Cacciamani, T.; Vita, A.; Cristalli, G.; Vincenzetti, S.; Natalini, P.; Ruggieri, S.; Amici, A.; Magni, G.
Purification of human cytidine deaminase: Molecular and enzymatic characterization and inhibition by synthetic pyrimidine analogs
Arch. Biochem. Biophys.
290
285-292
1991
Canis lupus familiaris, Gallus gallus, Escherichia coli, Homo sapiens, Mus musculus, no activity in Lactobacillus sp., no activity in Moraxella sp., no activity in Pseudomonas sp., Mus musculus BALB/c
Manually annotated by BRENDA team
Barchi, J.J.; Haces, A.; Marquez, V.E.; McCormack, J.J.
Inhibition of cytidine deaminase by derivatives of 1-(beta-D-ribofuranosyl)-dihydropyrimidin-2-one(zebularine)
Nucleosides Nucleotides
11
1781-1793
1992
Homo sapiens, Mus musculus, Mus musculus BALB/c
-
Manually annotated by BRENDA team
Bouffard, D.Y.; Laliberte, J.; Momparler, R.L.
Kinetic studies on 2',2'-difluorodeoxycytidine (gemcitabine) with purified human deoxycytidine kinase and cytidine deaminase
Biochem. Pharmacol.
45
1857-1861
1993
Homo sapiens
Manually annotated by BRENDA team
Vincenzetti, S.; Cambi, A.; Neuhard, J.; Garattini, E.; Vita, A.
Recombinant human cytidine deaminase: Expression, purification, and characterization
Protein Expr. Purif.
8
247-253
1996
Bacillus subtilis, Escherichia coli, Homo sapiens, Escherichia coli DH5-alpha
Manually annotated by BRENDA team
Vincenzetti, S.; Cambi, A.; Balducci, E.; Natalini, P.; Volpini, R.; Vita, A.
Human placenta cytidine deaminase: A zinc metalloprotein
Biochemistry
42
469-476
1997
Bacillus subtilis, Homo sapiens
Manually annotated by BRENDA team
Carlow, D.C.; Carter, C.W.; Mejlhede, N.; Neuhard, J.; Wolfenden, R.
Cytidine deaminases from B. subtilis and E. coli: Compensating effects of changing zinc coordination and quaternary structure
Biochemistry
38
12258-12265
1999
Bacillus subtilis, Escherichia coli, Homo sapiens, Escherichia coli SO268
Manually annotated by BRENDA team
Faivre-Nitschke, E.; Grienenberger, J.M.; Gualberto, J.M.
A prokaryotic-type cytidine deaminase from Arabidopsis thaliana gene expression and functional characterization
Eur. J. Biochem.
263
896-903
1999
Arabidopsis thaliana, Bacillus subtilis, Saccharomyces cerevisiae, Brugia pahangi, Caenorhabditis elegans, Escherichia coli, Haemophilus influenzae, Homo sapiens, Mycoplasma pneumoniae, Escherichia coli BL21(D3)
Manually annotated by BRENDA team
Vincenzetti, S.; de Sanctis, G.; Costanzi, S.; Cristalli, G.; Mariani, P.; Mei, G.; Neuhard, J.; Natalini, P.; Polzonetti, V.; Vita, A.
Functional properties of subunit interactions in human cytidine deaminase
Protein Eng.
16
1055-1061
2003
Homo sapiens
Manually annotated by BRENDA team
Chung, S.J.; Fromme, J.C.; Verdine, G.L.
Structure of human cytidine deaminase bound to a potent inhibitor
J. Med. Chem.
48
658-660
2005
Homo sapiens
Manually annotated by BRENDA team
Costanzi, S.; Vincenzetti, S.; Cristalli, G.; Vita, A.
Human cytidine deaminase: A three-dimensional homology model of a tetrameric metallo-enzyme inferred from the crystal structure of a distantly related dimeric homologue
J. Mol. Graph. Model.
25
10-16
2006
Homo sapiens
Manually annotated by BRENDA team
Vincenzetti, S.; Mariani, P.L.; Cammertoni, N.; Polzonetti, V.; Natalini, P.; Quadrini, B.; Volpini, R.; Vita, A.
Isoenzymatic forms of human cytidine deaminase
Protein Eng. Des. Sel.
17
871-877
2004
Homo sapiens
Manually annotated by BRENDA team
Lemaire, M.; Momparler, L.F.; Raynal, N.J.; Bernstein, M.L.; Momparler, R.L.
Inhibition of cytidine deaminase by zebularine enhances the antineoplastic action of 5-aza-2-deoxycytidine
Cancer Chemother. Pharmacol.
63
411-416
2009
Homo sapiens
Manually annotated by BRENDA team
Matsubara, T.; Dupuis, M.; Aida, M.
The ONIOM molecular dynamics method for biochemical applications: cytidine deaminase
Chem. Phys. Lett.
437
138-142
2007
Homo sapiens
-
Manually annotated by BRENDA team
Vincenzetti, S.; Quadrini, B.; Mariani, P.; De Sanctis, G.; Cammertoni, N.; Polzonetti, V.; Pucciarelli, S.; Natalini, P.; Vita, A.
Modulation of human cytidine deaminase by specific amino acids involved in the intersubunit interactions
Proteins
70
144-156
2007
Homo sapiens
Manually annotated by BRENDA team
Sigmond, J.; Honeywell, R.J.; Postma, T.J.; Dirven, C.M.; de Lange, S.M.; van der Born, K.; Laan, A.C.; Baayen, J.C.; Van Groeningen, C.J.; Bergman, A.M.; Giaccone, G.; Peters, G.J.
Gemcitabine uptake in glioblastoma multiforme: potential as a radiosensitizer
Ann. Oncol.
20
182-187
2009
Homo sapiens
Manually annotated by BRENDA team
Besnard, T.; Renee, N.; Etienne-Grimaldi, M.; Francois, E.; Milano, G.
Optimized blood sampling with cytidine deaminase inhibitor for improved analysis of capecitabine metabolites
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
870
117-120
2008
Homo sapiens
Manually annotated by BRENDA team
Giovannetti, E.; Laan, A.C.; Vasile, E.; Tibaldi, C.; Nannizzi, S.; Ricciardi, S.; Falcone, A.; Danesi, R.; Peters, G.J.
Correlation between cytidine deaminase genotype and gemcitabine deamination in blood samples
Nucleosides Nucleotides Nucleic Acids
27
720-725
2008
Homo sapiens
Manually annotated by BRENDA team
Tibaldi, C.; Camerini, A.; Tiseo, M.; Mazzoni, F.; Barbieri, F.; Vittimberga, I.; Brighenti, M.; Boni, L.; Baldini, E.; Gilli, A.; Honeywell, R.; Chartoire, M.; Peters, G.J.; Giovannetti, E.; Giovannetti, E.
Cytidine deaminase enzymatic activity is a prognostic biomarker in gemcitabine/platinum-treated advanced non-small-cell lung cancer a prospective validation study
Br. J. Cancer
119
1326-1331
2018
Homo sapiens (P32320), Homo sapiens
Manually annotated by BRENDA team
Furusho, K.; Shibata, T.; Sato, R.; Fukui, R.; Motoi, Y.; Zhang, Y.; Saitoh, S.I.; Ichinohe, T.; Moriyama, M.; Nakamura, S.; Miyake, K.
Cytidine deaminase enables Toll-like receptor 8 activation by cytidine or its analogs
Int. Immunol.
31
167-173
2019
Homo sapiens (P32320)
Manually annotated by BRENDA team