Information on EC 3.5.4.5 - cytidine deaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.5.4.5
-
RECOMMENDED NAME
GeneOntology No.
cytidine deaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2'-deoxycytidine + H2O = 2'-deoxyuridine + NH3
show the reaction diagram
(2)
-
-
-
cytidine + H2O = uridine + NH3
show the reaction diagram
(1)
-
-
-
cytidine + H2O = uridine + NH3
show the reaction diagram
quantum chemical study on mechanism, the extra water molecule from solvent may support catalysis. Proposal of catalytic cycle
P0ABF6
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
amidine hydrolysis
-
-
Deamination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
pyrimidine deoxyribonucleosides degradation
-
pyrimidine deoxyribonucleosides salvage
-
pyrimidine ribonucleosides degradation
-
pyrimidine ribonucleosides salvage I
-
pyrimidine ribonucleosides salvage II
-
Pyrimidine metabolism
-
Drug metabolism - other enzymes
-
Metabolic 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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A3DE
-
gene name
activation-induced cytidine deaminase
-
-
-
-
activation-induced cytidine deaminase
-
-
activation-induced cytidine deaminase
-
-
activation-induced deaminase
-
-
activation-induced deoxycytidine deaminase
-
-
AICDA
-
-
-
-
AICDA
-
gene name
Apo3G
-
-
APOBEC3
-
-
APOBEC3G
-
-
APOBEC3G cytidine deaminase
-
-
canine hepatic cyd deaminase
-
-
CDA
Bacillus caldolyticus DSM405 (T53)
-
-
-
CDA
Geobacillus stearothermophilus IFO12550 (T101)
-
-
-
CDABcald
Q9R2S1
-
CR deaminase
-
-
Cytidine aminohydrolase
-
-
-
-
cytidine deaminase
-
-
cytidine/2'-deoxycytidine aminohydrolase
-
-
cytidine/2'-deoxycytidine aminohydrolase
Bacillus caldolyticus DSM405 (T53)
-
-
-
cytidine/2'-deoxycytidine aminohydrolase
-
-
cytidine/2'-deoxycytidine aminohydrolase
Geobacillus stearothermophilus IFO12550 (T101)
-
-
-
cytidine/2'-deoxycytidine aminohydrolase
-
-
cytosine nucleoside deaminase
-
-
-
-
DCD
-
-
-
-
dCDA
-
-
-
-
dCDA
-
-
DNA cytidine deaminase
-
-
mammalian deminase
-
-
mammalian deminase
Mus musculus BALB/c
-
-
-
single-stranded DNA deoxycytidine deaminase
-
-
single-stranded DNA-dependent deoxycytidine deaminase
-
-
ssDNA deoxycytidine deaminase
-
-
T-CDA
-
-
yeast cytidine deaminase
-
-
mammalian deminase
-
-
additional information
-
cf. EC 3.5.4.14; cf. EC 3.5.4.5
CAS REGISTRY NUMBER
COMMENTARY
37259-56-6
-
9025-06-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
Bacillus caldolyticus DSM405 (T53)
-
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
mosquito parasite
-
-
Manually annotated by BRENDA team
mutant H102N
-
-
Manually annotated by BRENDA team
strain 15 (ATCC 9723)
-
-
Manually annotated by BRENDA team
strain A19
-
-
Manually annotated by BRENDA team
strain BL21(D3)
-
-
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain JF611
-
-
Manually annotated by BRENDA team
strain SO268
-
-
Manually annotated by BRENDA team
strain SO5201
-
-
Manually annotated by BRENDA team
strain Y-70-272
-
-
Manually annotated by BRENDA team
Escherichia coli 15 (ATCC 9723)
strain 15 (ATCC 9723)
-
-
Manually annotated by BRENDA team
Escherichia coli A19
strain A19
-
-
Manually annotated by BRENDA team
Escherichia coli BL21(D3)
strain BL21(D3)
-
-
Manually annotated by BRENDA team
Escherichia coli DH5-alpha
strain DH5alpha
-
-
Manually annotated by BRENDA team
Escherichia coli JF611
strain JF611
-
-
Manually annotated by BRENDA team
Escherichia coli SO268
strain SO268
-
-
Manually annotated by BRENDA team
Escherichia coli SO5201
strain SO5201
-
-
Manually annotated by BRENDA team
Escherichia coli Y-70-272
strain Y-70-272
-
-
Manually annotated by BRENDA team
Felis catus domesticus
cat
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus IFO12550 (T101)
-
-
-
Manually annotated by BRENDA team
expression in mouse
-
-
Manually annotated by BRENDA team
gene A3DE
-
-
Manually annotated by BRENDA team
glioblastoma multiforme (GBM) patients
-
-
Manually annotated by BRENDA team
HeLa cells; human
-
-
Manually annotated by BRENDA team
hematopoietic cell lines; human
-
-
Manually annotated by BRENDA team
rhesus monkey
-
-
Manually annotated by BRENDA team
BALB/c; mouse; Swiss-Webster strain DBA/2
-
-
Manually annotated by BRENDA team
gene Aicda
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv3315c
-
O53367
Uniprot
Manually annotated by BRENDA team
no activity in Lactobacillus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Moraxella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Moraxella sp.
Neisseria meningitidis
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
P. acidovorans
-
-
Manually annotated by BRENDA team
strain CT16
-
-
Manually annotated by BRENDA team
Nocardioides sp. CT16
strain CT16
-
-
Manually annotated by BRENDA team
strain NRC-510, grown on nitrate
-
-
Manually annotated by BRENDA team
Penicillium palitans NRC-510
strain NRC-510, grown on nitrate
-
-
Manually annotated by BRENDA team
frog
-
-
Manually annotated by BRENDA team
brewers' yeast
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
human pathogen, Culbertson strain, epimastigotes, ATCC 30013
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
an active-site Thr/Ser is conserved in mammalian DNA cytidine deaminases, overview
evolution
-
APOBEC3G belongs to an APOBEC superfamily containing at least 11 members
malfunction
-
loss-of-function mutations of AID fail to undergo SHM
malfunction
-
cytidine deaminase-deficient APOBEC3G lacks antiviral activity when expressed within physiological levels in T cells
malfunction
-
phospho-mimetic variants fail to mediate isotype switching in activated mouse splenic B lymphocytes or suppress HIV-1 replication in human T cells. Phospho-null alanine mutants maintain intrinsic DNA deaminase activity, whereas phosphomimetic glutamate mutants are inactive
malfunction
-
patients with hyper-IgM syndromes who are deficient in activation-induced cytidine deaminase, which is required for class switch recombination and somatic hypermutation, are prone to develop autoimmune diseases. Defective peripheral B-cell tolerance checkpoint occurs in AID-deficient patients, overview
malfunction
-
impaired central B-cell tolerance and increased serum autoAb in Aicda-/- mice compared to the wild-type
malfunction
-
CD domain switch or replacement greatly affect the sensitivity to Vif induced degradation, editing and antiviral activity of hA3G, but the replacement or switch of CDs has no effect on hA3G viral incorporation, overview. The mutants show a nucleotide sequence preference pattern
metabolism
-
CDA is a pyrimidine salvage pathway enzyme that recycles cytidine and 20-deoxycytidine for uridine and 2-deoxyuridine synthesis, respectively
physiological function
C0IL37, -
CDA is involved in the immune response of gastropod abalone
physiological function
-
AID is necessary for adaptive immunity. AID is used to initiate affinity maturation of antibodies by deaminating immunoglobulin G genes in germinal center B-cells in order to initiate antibody diversification pathways for somatic hypermutation and class switch recombination
physiological function
-
AID is an essential factor for the class switch recombination and somatic hypermutation of immunglobulin genes. The C-terminal domain of AID is not required for S-region DNA breaks but is required for S-region recombination after DNA cleavage. Class switch recombination, but not somatic hypermutation, is dependent on the nuclear export of AID
physiological function
-
cytidine deamination is the primary mechanism by which APOBEC3G restricts HIV-1
physiological function
-
cytidine amidase is involved in the hydrolytic deamination of cytidine or 2'-deoxycytidine to uridine or 2'-deoxyuridine, determination of the protein-ligand recognition process, respectively
physiological function
-
beneficial effects of DNA cytidine deamination by activation-induced deaminase, i.e. AID, and APOBEC3G. Probable contributions of the enzyme to carcinogenesis. Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
physiological function
-
A3DE exhibits relatively low levels of anti-human immunodeficiency virus type 1, anti-HIV-1, activity, Vif still neutralizes this activity. The A3DE region II is responsible for the low activity of A3DE
physiological function
-
AID is required for the establishment of both central and peripheral B-cell tolerance
physiological function
-
activation-induced cytidine deaminase initiates somatic hypermutation, class-switch recombination, and gene conversion of Ig genes by the deamination of deoxycytidine, followed by error-prone mismatch- or base-excision DNA repair. Aicda impairs B-cell development
physiological function
-
the two cytidine deaminase domains of the cytidine deaminase act as an anti-HIV-1 host factor. The two CD domains of A3G are functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif off A3G, overview
metabolism
-
cytidine deaminase is a key enzyme in the pyrimidine salvage pathway
additional information
-
sequence comparison of A3 proteins that have two cytidine deaminase, CDA, motifs, overview
additional information
-
HIV-1 Vif protein interacts with hA3G as a part of a Vif-Cul5-SCF complex, resulting in polyubiquitination and proteosomal degradation of hA3G. The hA3G/Vif interaction is a prerequisite for the degradation of hA3G
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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)-5-iodocytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine + H2O
?
show the reaction diagram
-
FIAC poorly deminated
-
-
?
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
-
araC, most effective agent in therapy of acute myeloblastic leukemia
-
-
?
1-beta-D-arabinofuranosylcytosine + H2O
?
show the reaction diagram
Escherichia coli DH5-alpha
-
-
-
-
?
2',2'-difluorodeoxycytidine + H2O
2',2'-difluorodeoxyuridine + NH3
show the reaction diagram
-
gemcitabine, antimetabolite of deoxycytidine, active against solid tumors and leukemic cell lines, deamination by the enzyme results in loss of pharmacologic activity
-
?
2',2'-difluorodeoxycytidine + H2O
2',2'-difluorodeoxyuridine + NH3
show the reaction diagram
-
deamination of the deoxynucleoside analogue gemcitabine (dFdC) to difluorodeoxyuridine (dFdU), difluorodeoxyuridine used as radiosensitizer in gene therapy
-
-
?
2',3'-dideoxycytidine + H2O
2',3'-dideoxyuridinel + NH3
show the reaction diagram
-
-
-
-
?
2',3'-dideoxycytidine + H2O
2',3'-dideoxyuridinel + NH3
show the reaction diagram
-
selective inhibitor of HIV reverse transcriptase
-
-
-
2',5'-anhydroarabinosylcytosine + H2O
2',5'-anhydroarabinosyluracil + NH3
show the reaction diagram
Mus musculus, Mus musculus BALB/c
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
P56389
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
P32320
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-, O53367
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
in ssDNA
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
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
-
-
-
-
?
2'-fluoro-2'-deoxycytidine + H2O
2'-fluoro-2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
2'-fluoro-2'-deoxycytidine + H2O
2'-fluoro-2'-deoxyuridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
2'-O-methylcytidine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-thio-cytidine + H2O
2'-thiouridine + NH3
show the reaction diagram
-
-
-
-
?
3'-amino-2',3'-dideoxycytidine + H2O
3'-amino-2',3'-dideoxyuridine + NH3
show the reaction diagram
-
-
-
?
5'-bromoarabinosylcytosine + H2O
5'-bromoarabinosyluracil + NH3
show the reaction diagram
-
-
-
-
?
5'-chloroarabinosylcytosine + H2O
5'-chloroarabinosyluracil + 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'-fluoro-5'-deoxycytidine + H2O
5'-fluoro-5'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5'-fluoro-5'-deoxycytidine + H2O
5'-fluoro-5'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5'-fluoro-5'-deoxycytidine + H2O
5'-fluoro-5'-deoxyuridine + NH3
show the reaction diagram
Escherichia coli Y-70-272
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
5'-methyl-2'-deoxycytidine + H2O
5'-methyl-2-deoxyuridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
5,6-dihydrocytidine + H2O
5,6-dihydrouridine + NH3
show the reaction diagram
-
-
-
-
-
5,6-dihydrocytidine + H2O
5,6-dihydrouridine + NH3
show the reaction diagram
-
-
-
-
?
5-aza-2'-deoxycytidine + H2O
5-aza-2'-deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
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
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
-
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
-
-
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
5-azacytidine + H2O
5-azauridine + NH3
show the reaction diagram
Escherichia coli BL21(D3)
-
-
-
-
?
5-azadeoxycytidine + H2O
5-azadeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-azadeoxycytidine + H2O
5-azadeoxyuridine + NH3
show the reaction diagram
P32320
-
-
-
?
5-azadeoxycytidine + H2O
5-azadeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-bromocytidine + H2O
5-bromouridine + NH3
show the reaction diagram
-
-
-
-
?
5-bromodeoxycytidine + H2O
5-bromodeoxyuridine + 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-iodocytidine + H2O
5-iodouridine + NH3
show the reaction diagram
-
-
-
-
?
5-iodocytidine + H2O
5-iodouridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
5-iododeoxycytidine + H2O
5-iododeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-iododeoxycytidine + H2O
5-iododeoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
5-methyl-dCMP + H2O
5-methyl-dCyd
show the reaction diagram
Nocardioides sp., Nocardioides sp. CT16
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
-
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
-
-
-
-
-
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
-
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
-
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
5-methylcytidine + H2O
5-methyluridine + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
6-azacytidine + H2O
6-azauridine + NH3
show the reaction diagram
-
-
-
-
?
bromodeoxycytidine + H2O
bromodeoxyuridine + NH3
show the reaction diagram
-
-
-
?
CTP + H2O
UTP + NH3
show the reaction diagram
Nocardioides sp., Nocardioides sp. CT16
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
P56389
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
P32320
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-, O53367
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Rana sp., Columba sp., Felis catus domesticus
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
C0IL37, -
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
cytidine deaminase is a key enzyme in the catabolism of cytosine nucleoside analogues, since their deamination results in a loss of their pharmacological activity
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
P56389
cytidine is distinguished from uridine by its 4-NH2 group that acts as a hydrogen bond donor, the charge-neutralizing Arg68 of CDA exhibits two alternate conformations I and II, binding structure, overview
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
development and implementation of the ONIOM-molecular dynamics method with cytidine deaminase as model enzyme for determination of activity and biochemical properties, product uridine is strongly perturbed by the thermal motion of the environment and dissociates easily from the active site, overview
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Bacillus caldolyticus DSM405 (T53)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Geobacillus stearothermophilus IFO12550 (T101)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli DH5-alpha
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli SO268
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli 15 (ATCC 9723)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli A19
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli BL21(D3)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli Y-70-272
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
P32320
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
Escherichia coli BL21(D3)
-
-
-
-
?
cytosine arabinoside + H2O
uridine arabinoside + NH3
show the reaction diagram
Escherichia coli Y-70-272
-
-
-
-
?
cytosine arabinoside + H2O
?
show the reaction diagram
-
-
-
?
cytosine arabinoside + H2O
?
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dUTP + NH3
show the reaction diagram
Nocardioides sp., Nocardioides sp. CT16
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-, Q9R2S1
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Q9S3M0, -
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Escherichia coli DH5-alpha
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Escherichia coli BL21(D3)
-
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
Escherichia coli Y-70-272
-
-
-
-
?
N-4-monoacetylarabinosylcytosine
uracil arabinoside + carbamate
show the reaction diagram
Mus musculus, Mus musculus BALB/c
-
-
-
-
?
N4-methylcytidine + H2O
uridine + methylamine
show the reaction diagram
-
-
-
-
r
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
?
-
-
-
-
-
-
additional information
?
-
-
3-methylcytidine, cytosine and cyclocytidine are no substrates
-
-
-
additional information
?
-
-
cytosine and cytosine nucleotides are no substrates
-
-
-
additional information
?
-
-
6-methylcytidine is no substrate
-
-
-
additional information
?
-
-
cyclocytidine, N-4-acetylarabinosylcytosine, tetraacetylarabinosylcytosine, N4-behenoylarabinosylcytosine and tri-O-acetylarabinosylcytosine are no substrates
-
-
-
additional information
?
-
-
cytosine, 5-methylcytosine, 6-methylaminopurine, CMP, dCMP, CDP, dCDP, CTP and dCTP are no substrates
-
-
-
additional information
?
-
-
cytosine and cytidine nucleosides are not deaminated by this enzyme
-
-
-
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
cytidine deaminase plays an important role in the activation of the anticancer drug capesitabine in the human body
-
-
-
additional information
?
-
P56389
active site and substrate binding structure, overview
-
-
-
additional information
?
-
-
AID shows specific activity for ssDNA deamination
-
-
-
additional information
?
-
-
APOBEC3G cytidine deaminase contracts ssDNA in a deamination motif-dependent manner, presence of bidirectional quasi-localized scanning of APOBEC3G cytidine deaminase occurring proximal to a 5' hot motif, a motif-dependent DNA contraction greatest for 5' hot before 3' hot before 5' cold motifs, and diminished mobility at low salt, overview
-
-
-
additional information
?
-
-
the preferred sequence context for wild-type hA3G is GG. In the CD2-1 mutant variants, both TGG and GGG are preferred, while the wild-type prefers TGG
-
-
-
additional information
?
-
Mus musculus BALB/c
-
cytosine, 5-methylcytosine, 6-methylaminopurine, CMP, dCMP, CDP, dCDP, CTP and dCTP are no substrates
-
-
-
additional information
?
-
Mus musculus BALB/c
-
cyclocytidine, N-4-acetylarabinosylcytosine, tetraacetylarabinosylcytosine, N4-behenoylarabinosylcytosine and tri-O-acetylarabinosylcytosine are no substrates
-
-
-
additional information
?
-
Escherichia coli A19
-
6-methylcytidine is no substrate
-
-
-
additional information
?
-
Escherichia coli Y-70-272
-
cytosine and cytidine nucleosides are not deaminated by this enzyme
-
-
-
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
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
P56389
-
-
-
?
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
in ssDNA
-
-
?
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
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
P56389
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Rana sp., Columba sp., Felis catus domesticus
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
C0IL37, -
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
cytidine deaminase is a key enzyme in the catabolism of cytosine nucleoside analogues, since their deamination results in a loss of their pharmacological activity
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli JF611
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli DH5-alpha
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli SO5201
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli SO268
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli 15 (ATCC 9723)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli A19
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli BL21(D3)
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
Escherichia coli Y-70-272
-
-
-
-
?
cytosine arabinoside + H2O
?
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
show the reaction diagram
-
-
-
?
deoxycytidine + H2O
deoxyuridine + NH3
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 ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
1 mM, activity 101%
Mg2+
-
activation
Mg2+
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
Mn2+
-
10 mM, activity 106%
Mn2+
-
-
Mn2+
-
slight activation
NaCl
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
Zinc
-
wild-type enzyme and mutant enzymes R56A, R56Q and C53H/R56Q contain about 1 mol of zinc per subunit. Mutant enzyme R56D contains 0.2 mol of zinc per subunit
Zn2+
-
1 mM, activity 103%
Zn2+
-
1 M tightly bound zinc per enzyme subunit, activated by added zinc
Zn2+
-
contains 4 Zn2+ per tetramer. The role of Zn2+ is to activate a water molecule and thereby generate a hydroxide ion
Zn2+
P56389
catalytic ion, coordinated by C65, C99, and C102; dependent on
Zn2+
-
-
Zn2+
C0IL37, -
zinc-dependent enzyme
Zn2+
-
CDA is a zinc-dependent metalloenzyme and contains one mol of Zn2+ per mol of enzyme subunit
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(cytidyl)acryloylaminohexanoic acid
-
i.e. CV6
1,10-phenanthroline
-
-
1-(beta-D-ribofuranosyl)-dihydropyrimidine-2-one
-
zebularine
1-(beta-D-ribofuranosyl)-dihydropyrimidine-2-one
-
-
1-methyladenosine
-
competitive inhibition
2'-Deoxyuridine
-
-
2'-deoxyzebularine 5'-monophosphate
-
-
2-beta-D-ribofuranosyl-1,2,4-triazol-3-one
-
-
2-mercaptoethanol
-
-
2-thio-6-azarudine
-
-
3'-azido-3'-deoxythymidine
-
-
3,4,5,6,tetrahydrozebularine
-
-
3,4,5,6-Tetrahydrouridine
-
potent competitive inhibitor
3,4,5,6-Tetrahydrouridine
-
potent competitive inhibitor
3,4,5,6-Tetrahydrouridine
-
recombinant CDA
3,4,5,6-Tetrahydrouridine
-
-
3,4,5,6-Tetrahydrouridine
-
-
3,4,5,6-Tetrahydrouridine
-
-
3,4,5,6-Tetrahydrouridine
-
i.e. THU
3,4,5,6-Tetrahydrouridine
-
-
3-deazauridine
-
-
3-deazauridine
-
recombinant enzyme
3-deazauridine
-
-
3-deazauridine
P56389
-
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
-
competitive inhibition
5,6-Dihydrouridine
-
-
5-(Chloromercuri)cytidine
-
-
5-bromodeoxyuridine
-
-
5-bromodeoxyuridine
-
1.0 mM, 31% inhibition
5-bromodeoxyuridine
-
-
5-Bromouridine
-
-
5-fluoro-2'-deoxyuridine
-
-
5-fluoro-2'-deoxyuridine
-
recombinant enzyme
5-fluoro-2'-deoxyuridine
-
-
5-fluoropyrimidin-2-one ribonucleoside
-
-
5-fluorouridine
-
-
5-fluorouridine
-
-
5-iodo-2'-deoxyuridine
-
-
5-methyluridine
-
-
5-{(1E)-3-[(5-carboxypentyl)amino]-3-oxoprop-1-en-1-yl}-5,6-dihydrocytidine
-
-
5-{(1E)-3-[(5-carboxypentyl)amino]-3-oxoprop-1-en-1-yl}-5,6-dihydrocytidine
-
recombinant enzyme
5-{(1E)-3-[(5-carboxypentyl)amino]-3-oxoprop-1-en-1-yl}-5,6-dihydrocytidine
-
-
6-azauridine
-
-
6-Thioguanine
-
-
6-[3,5(cytidyl)acryloylamino] hexanoic acid
P32320
-
6-[3-(5-cytidyl)acryloylamino]hexanoic acid
-
i.e. CV6
adenosine
-
4.0 mM, 22% inhibition
CMP
-
0.300 mM 50% inhibition, 0.750 mM 90% inhibition
CMP
-
recombinant CDA
CuSO4
-
complete inhibition
cytidine
-
strong substrate inhibition above 0.5 mM
cytidine monophosphate
-
-
deoxyadenosine
-
3.0 mM, 32% inhibition
deoxyadenosine
-
competitive inhibition
deoxyguanosine
-
1.0 mM, 13% inhibition
deoxyguanosine
-
-
Deoxyuridine
-
-
Deoxyuridine
-
1.0 mM, 32% inhibition
Deoxyuridine
-
competitive inhibition
diazepinone riboside
-
-
diazepinone riboside
-
inhibitor is able to establish a canonical pi/pi interaction with key active site residue F137
dihydrothymidine
-
competitive inhibition
dipicolinic acid
-
-
dithiothreitol
-
-
dTMP
-
0.400 mM 50% inhibition
dTTP
-
0.400 mM 50% inhibition
GTP
-
0.750 mM 85% inhibition
guanosine
-
1.0 mM, 4% inhibition
HgCl2
-
complete inhibition
mercaptoethanol
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
weak inhibition
N-ethylmaleimide
-
-
NH3
-
product inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-mercuribenzoate
-
highly sensitive
p-mercuribenzoate
-
highly sensitive
p-mercuribenzoate
-
enzyme from leukemic spleen, enzyme from normal spleen is much less sensitive
p-mercuribenzoate
-
-
phosphapyrimidine
-
-
phosphapyrimidine nucleoside
-
-
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
P56389
-
tetrahydrouridine
-
i.e. THU, acts as as a transition-state analogue of the natural substrate cytidine, quantitative determination of the cytidine deaminase inhibitor in mouse plasma by liquid chromatography/electrospray ionization tandem mass spectrometry, pharmacokinetics, overview
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
thioglycolic acid
-
0.7 mM 88% relative activity, complete inhibition at 7 mM
thymidine
-
1.0 mM, 21% inhibition
thymidine
-
competitive inhibition
thymine riboside
-
competitive inhibition
thymine riboside
-
-
thymine riboside
-
recombinant CDA
thymine riboside
-
-
thymine riboside
-
-
uracil arabinoside
-
4.0 mM, 48% inhibition
Urea
-
above 2 M, reversible inactivation
uridine
-
-
uridine
-
4.0 mM, 20% inhibition
uridine
-
inhibition relatively slow
uridine
-
product inhibition
uridine
-
recombinant enzyme
uridine
-
product inhibition
UTP
-
recombinant CDA
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
Zn2+
-
above 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5-fluorozebularine
P32320
the presence of 5-fluorozebularine in the growth medium enhances of 2-3folds the specific activity of the Y33G mutant enzyme
bromodeoxyuridine
-
-
cytidine
P32320
the presence of cytidine in the growth medium enhances of 2-3folds the specific activity of the Y33G mutant enzyme
dithiothreitol
-
-
EDTA
-
10 mM, activity 108%
N-ethylmaleimide
-
0.10-0.20 mM, activity 114%
p-chloromercuribenzoate
-
0.105 mM, activity 112%
uridine
P32320
the presence of uridine in the growth medium enhances of 2-3folds the specific activity of the Y33G mutant enzyme
iodoacetic acid
-
0.10 mM, activity 105%
additional information
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.31
-
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine
-
leukemia enzyme
2.8
-
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine
-
-
3.9
-
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-iodocytosine
-
-
0.33
-
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
-
-
0.66
-
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
-
-
0.27
-
1-beta-D-arabinofuranosylcytosine
-
-
0.51
-
1-beta-D-arabinofuranosylcytosine
-
-
0.0092
-
2',2'-difluorodeoxycytidine
-
i.e. gemcitabine, variation of plasma gemcitabine between 0.9 and 9.2 microM
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
-
2'-deoxycytidine
-
pH 7.5, 37C, recombinant mutant R68G
0.03
-
2'-deoxycytidine
-
native enzyme, 37C
0.039
-
2'-deoxycytidine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.039
-
2'-deoxycytidine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.04
-
2'-deoxycytidine
-
tetramer of recombinant subunit CDA2, 37C
0.042
-
2'-deoxycytidine
-
tetramer of recombinant subunit CDA1, 37C
0.0476
-
2'-deoxycytidine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.051
-
2'-deoxycytidine
-
pH 7.5, 37C, recombinant mutant R68Q
0.058
-
2'-deoxycytidine
-
-
0.4
-
2'-deoxycytidine
-
pH 7.5, 37C, recombinant mutant Y60G
1.059
-
2'-deoxycytidine
-
in 50 mM Tris-HCl buffer pH 7.5 at 25C
0.07
-
2'-fluoro-2'-deoxy-5-iodocytosine arabinoside
-
-
0.091
-
2-deoxycytidine
-
-
0.087
-
5'-fluoro-5'-deoxycytidine
-
-
0.11
-
5,6-Dihydrocytidine
-
-
0.113
-
5,6-Dihydrocytidine
-
-
0.0477
-
5-aza-2'-deoxycytidine
-
pH 7.4, 37C
0.058
-
5-azacytidine
-
-
0.28
-
5-azacytidine
-
recombinant CDA
0.28
-
5-azacytidine
-
tetramer of recombinant subunit CDA2, 37C
0.31
-
5-azacytidine
-
recombinant AT-CDA
0.31
-
5-azacytidine
-
tetramer of recombinant subunit CDA1, 37C
2.27
-
5-azacytidine
-
-
0.0748
-
5-azadeoxycytidine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.349
-
5-azadeoxycytidine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.087
-
5-iododeoxycytidine
-
tetramer of recombinant subunit CDA1, 37C
0.1
-
5-iododeoxycytidine
-
recombinant CDA
0.1
-
5-iododeoxycytidine
-
tetramer of recombinant subunit CDA2, 37C
0.13
-
5-methyl-dCMP
-
pH 7.0, 37C
0.04
-
5-methylcytidine
-
recombinant CDA
0.58
-
5-methylcytidine
-
recombinant
0.95
-
5-methylcytidine
-
-
1.25
-
5-methylcytidine
-
-
0.06
-
5-Methyldeoxycytidine
-
-
4.2
-
6-azacytidine
-
-
0.14
-
CMP
-
pH 7.0, 37C
0.0092
-
cytidine
-
-
0.0167
-
cytidine
-
nonhomogenous enzyme
0.031
-
cytidine
-
pH 7.5, 37C, recombinant mutant R68G
0.039
-
cytidine
-
recombinant CDA
0.039
-
cytidine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.039
-
cytidine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.04
-
cytidine
-
tetramer of recombinant subunit CDA1, 37C
0.042
-
cytidine
-
tetramer of recombinant subunit CDA2, 37C
0.049
-
cytidine
-
-
0.05
-
cytidine
-
-
0.063
-
cytidine
-
normal and leukemic spleen enzyme
0.0745
-
cytidine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.091
-
cytidine
-
at pH 6
0.11
-
cytidine
-
at pH 7.5
0.11
-
cytidine
-
-
0.118
-
cytidine
-
pH 7.5, 37C, recombinant mutant R68Q
0.12
-
cytidine
-
wild-type
0.129
-
cytidine
-
-
0.14
-
cytidine
-
pH 7.6, 25C, mutant enzyme R56A
0.15
-
cytidine
-
recombinant AT-CDA
0.167
-
cytidine
-
-
0.174
-
cytidine
-
-
0.18
-
cytidine
-
-
0.2
-
cytidine
-
at pH 7.5 with H2O and pH 8.4 with H2O or D2O
0.2
-
cytidine
-
mutant H102N
0.208
-
cytidine
-
at pH 7.5 with D2O
0.21
-
cytidine
-
-
0.216
-
cytidine
-
pH 7.6, 25C, wild-type enzyme
0.22
-
cytidine
-
-
0.233
-
cytidine
-
at pH 7.1 with D2O
0.238
-
cytidine
-
at pH 7.1 with D2O
0.25
-
cytidine
-
mutant H102Q
0.267
-
cytidine
-
pH 7.6, 25C, mutant enzyme R56Q
0.27
-
cytidine
-
pH 7.5, 37C, recombinant mutant Y60G
0.39
-
cytidine
-
mutant H102A
1.004
-
cytidine
-
in 50 mM Tris-HCl buffer pH 7.5 at 25C
1.5
-
cytidine
-
mutant C129A
1.8
1.9
cytidine
-
radioactive labeled substrate
2.2
-
cytidine
-
homogenous preparation
6.6
-
cytidine
-
amplified gene, pH 7.0, 37C
0.089
-
cytosine
-
-
0.058
-
cytosine arabinoside
-
recombinant AT-CDA
0.11
-
cytosine arabinoside
-
recombinant CDA
0.11
-
cytosine arabinoside
-
tetramer of recombinant subunit CDA2, 37C
0.11
-
cytosine arabinoside
-
pH 7.5, 37C, recombinant wild-type enzyme
0.11
-
cytosine arabinoside
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.14
-
cytosine arabinoside
-
-
0.15
-
cytosine arabinoside
-
tetramer of recombinant subunit CDA1, 37C
0.15
-
cytosine arabinoside
-
pH 7.5, 37C, recombinant mutant R68G
0.19
-
cytosine arabinoside
-
pH 7.5, 37C, recombinant mutant R68Q
0.22
-
cytosine arabinoside
-
-
0.26
-
cytosine arabinoside
-
-
0.385
-
cytosine arabinoside
-
pH 7.5, 37C, recombinant mutant Y60G
0.089
-
cytosine deoxyriboside
-
-
0.055
-
dCMP
-
pH 7.0, 37C
0.0075
-
Deoxycytidine
-
pH 7.8, 25C, mutant enzyme R56A
0.029
-
Deoxycytidine
-
pH 7.8, 25C, mutant enzyme R56Q
0.039
-
Deoxycytidine
-
recombinant CDA
0.0463
-
Deoxycytidine
-
-
0.055
-
Deoxycytidine
-
-
0.06
-
Deoxycytidine
-
-
0.075
-
Deoxycytidine
-
recombinant AT-CDA
0.079
-
Deoxycytidine
-
leukemic spleen enzyme
0.0853
-
Deoxycytidine
-
-
0.09
0.1
Deoxycytidine
-
-
0.09
-
Deoxycytidine
-
-
0.12
-
Deoxycytidine
-
recombinant At-CDA1
0.21
-
Deoxycytidine
-
amplified gene
0.236
-
Deoxycytidine
-
pH 7.8, 25C, wild-type enzyme
0.34
-
Deoxycytidine
-
leukemic spleen enzyme
0.58
-
Deoxycytidine
-
-
1.8
1.9
Deoxycytidine
-
radioactive labeled substrate
8.53
-
Deoxycytidine
-
-
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
-
additional information
-
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
-
additional information
-
additional information
-
wild-type AID and active and inactive point mutants bind cooperatively to ssDNA with Hill coefficients of about 1.7-3.2 and with microscopic dissociation constant values (KA) ranging between 10 and 250 nM. Active C-terminal deletion mutants bind ssDNA non-cooperatively with KA values similar to wild-type AID
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.5
-
2'-deoxycytidine
-
in 50 mM Tris-HCl buffer pH 7.5 at 25C
4.8
-
cytidine
-
in 50 mM Tris-HCl buffer pH 7.5 at 25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.034
-
(cytidyl)acryloylaminohexanoic acid
-
tetramer of recombinant subunit CDA1, 37C
0.045
-
(cytidyl)acryloylaminohexanoic acid
-
tetramer of recombinant subunit CDA2, 37C
0.00042
-
3,4,5,6-Tetrahydrouridine
-
pH 7.5, 37C, recombinant mutant R68Q
0.0067
-
3,4,5,6-Tetrahydrouridine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.0067
-
3,4,5,6-Tetrahydrouridine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.007
-
3,4,5,6-Tetrahydrouridine
-
tetramer of recombinant subunit CDA1, 37C; tetramer of recombinant subunit CDA2, 37C
0.008
-
3,4,5,6-Tetrahydrouridine
-
pH 7.5, 37C, recombinant mutant Y60G
0.0256
-
3,4,5,6-Tetrahydrouridine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.015
-
5,6-Dihydrouridine
-
tetramer of recombinant subunit CDA1, 37C
0.04
-
5,6-Dihydrouridine
-
tetramer of recombinant subunit CDA2, 37C
0.00006
-
5-fluorozebularine
-
tetramer of recombinant subunit CDA1, 37C
0.0002
-
5-fluorozebularine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.0003
-
5-fluorozebularine
-
tetramer of recombinant subunit CDA2, 37C
0.0003
-
5-fluorozebularine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.0003
-
5-fluorozebularine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.0006
-
5-fluorozebularine
-
pH 7.5, 37C, recombinant mutant R68Q
0.0017
-
5-fluorozebularine
-
pH 7.5, 37C, recombinant mutant Y60G
0.0034
-
6-[3,5(cytidyl)acryloylamino] hexanoic acid
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.045
-
6-[3,5(cytidyl)acryloylamino] hexanoic acid
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.015
-
6-[3-(5-cytidyl)acryloylamino]hexanoic acid
-
pH 7.5, 37C, recombinant mutant Y60G
0.045
-
6-[3-(5-cytidyl)acryloylamino]hexanoic acid
-
pH 7.5, 37C, recombinant wild-type enzyme
0.3
-
cytidine monophosphate
-
tetramer of recombinant subunit CDA2, 37C
0.39
-
cytidine monophosphate
-
tetramer of recombinant subunit CDA1, 37C
0.000025
-
diazepinone riboside
-
-
0.0212
-
uridine
P32320
mutant enzyme Y33G, at 37C, pH not specified in the publication
0.1
-
uridine
-
pH 7.5, 37C, recombinant mutant Y60G
0.12
-
uridine
-
pH 7.5, 37C, recombinant mutant R68Q
0.31
-
uridine
-
tetramer of recombinant subunit CDA1, 37C; tetramer of recombinant subunit CDA2, 37C
0.4
-
uridine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.4
-
uridine
P32320
wild type enzyme, at 37C, pH not specified in the publication
0.00095
-
zebularine
-
pH 7.4, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
1.68
-
-
crude extract, pH 7.5, at 25C, using 2'-deoxycytidine as substrate
2.35
-
-
crude extract, pH 7.5, at 25C, using cytidine as substrate
3.3
-
-
-
3.75
-
-
after 2.2fold purification, pH 7.5, at 25C, using 2'-deoxycytidine as substrate
3.96
-
-
sarcoma tumour
4
-
-
amplified gene, 5'-aza-2'-deoxycytidine as substrate
4.9
-
-
amplified gene, 2'-thiocytidine as substrate
5.44
-
-
after 2.3fold purification, pH 7.5, at 25C, using cytidine as substrate
23.9
-
-
amplified gene, 5'-methylcytidine as substrate
29
-
-
colon tumour
31.8
-
-
amplified gene, ara-cytidine as substrate
43
-
-
amplified gene, cytidine as substrate
47.9
-
-
amplified gene, 5'-methyl-2'-deoxycytidine as substrate
64.1
-
-
-
68.4
-
-
amplified gene, 2'-fluoro-2'-deoxycytidine as substrate
86.7
-
-
pancreas tumour
90
-
-
-
97.6
-
-
amplified gene, deoxycytidine as substrate
105
-
-
-
225
-
-
pH 7.0, 37C
738
-
-
ovarian tumour
3558
-
-
amplified gene
additional information
-
-
variation between 1.51 to 5.50 nmol/h/mg protein, about 100-fold lower than that in liver
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
identical rates of deamination of cytidine at pH 8 and pH 10
5.9
7.35
-
deamination rate 50% higher in phosphate buffers with pH 7.25-8.7
7.2
-
-
leukemic spleen enzyme
7.3
-
-
assay at
7.4
-
-
assay at
7.5
-
-
-
7.5
-
-
assay at
7.6
-
-
assay at
8
-
-
identical rates of deamination of cytidine at pH 5 and pH 10
8
-
-
assay at
10
-
-
-
10
-
-
identical rates of deamination of cytidine at pH 5 and pH 8
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
10.5
-
deoxycytidine as substrate, specific activity constant in this range, beyond these values irreversible inactivation occurs
3.5
10.5
-
deoxycytidine as substrate, beyond these values irreversible inactivation occurs
6.5
10.7
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 30C, 46C, and 62C
37
-
-
assay at
37
-
-
assay at
56
62
-, Q9R2S1
-
58
-
-
recombinant wild-type enzyme
70
-
P32320
wild type CDA
99
-
-
maximum of activity
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
70
Q9S3M0, -
6C: 45% of maximal activity, 70C: 35% of maximal activity
12
66
-
12C: about 55% of maximal activity, 66C: about 65% of maximal activity
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 30C, 46C, and 62C
34
74
-, Q9R2S1
34C: 45% of maximal activity, 74C: 70% of maximal activity
37
75
-
60% of maximal activity at 75C for the wild-type enzyme, 35% for mutant R68Q
40
62
-
heat treatment for 5 min at 50-60C completely abolishes CMP and substrate inhibition
70
75
P32320
wild type CDA shows an activity optimum at about 70C and the activity decreases above 75C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
tetramer of recombinant subunit CDA2, isoelectric focusing
4.55
4.9
-
5 different isoforms of native enzyme, isoelectric focusing
4.9
-
-, Q9R2S1
chromatofocusing
5
-
-
tetramer of recombinant subunit CDA1, isoelectric focusing
7.3
-
C0IL37, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
AID expression occurs first in pro-B cells and increases on further development, peak AID expression is in immature and T1 B cells from bone marrow, is lower in splenic T1 B cells, and decreases precipitously in the splenic transitional 2 and mature B-cell compartments
Manually annotated by BRENDA team
-
glioblastoma multiforme (GBM) patients
Manually annotated by BRENDA team
-
glioblastoma multiforme (GBM) patients
Manually annotated by BRENDA team
-
normal and leukemic
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
Cavia porcellus, Columba sp., Felis catus domesticus
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
peripheral blood
Manually annotated by BRENDA team
-
different arrangement of subunit isoforms CDA1 and CDA2 results in five isoforms differing only in isoelectric point, native and recombinant enzyme
Manually annotated by BRENDA team
-
normal and leukemic spleen
Manually annotated by BRENDA team
Mus musculus BALB/c
-
normal and leukemic spleen
-
Manually annotated by BRENDA team
additional information
-
AID cDNA is undetectable in totipotent hematopoietic progenitors, and in cells committed to the T lymphocyte or myeloid lineages
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inner-surface of cytoplasmic membrane
Manually annotated by BRENDA team
C0IL37, -
CDA is largely concentrated in the cytoplasm
Manually annotated by BRENDA team
Escherichia coli BL21(D3)
-
-
-
Manually annotated by BRENDA team
Escherichia coli JF611
-
inner-surface of cytoplasmic membrane
-
Manually annotated by BRENDA team
C0IL37, -
CDA is partially concentrated in the nuclei
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium marinum (strain ATCC BAA-535 / M)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16000
-
-
estimated from cDNA open reading frame coding for human cytidine deaminase
16000
-
-
His-tagged CDA, SDS-PAGE
16170
-
-
deduced from cDNA nucleotide sequence
32500
-
-
calculated from cDNA open reading frame
32560
-
-
calculated from cDNA open reading frame
32580
-
-
calculated from amino acid sequence
45000
-
-
gel filtration
51000
-
-
human granulocytes
52000
-
-
gel filtration
52000
-
-
gel filtration
52990
-
-
gel filtration
54000
-
-
gel filtration
56000
-
-
gel filtration, Sephacryl S-300
56000
-
-
-
56000
-
-
calculated from Stokes radius
57000
-
-
gel filtration
57000
-
-
gel filtration, homogenous preparation
57000
-
-
gel filtration
60000
-
-
gel filtration
62000
-
-
gel filtration, native enzyme
63000
-
-
gel filtration
66000
-
-
gel filtration, SDS-PAGE
73000
-
-
gel filtration, nonhomogenous preparation
74000
-
-
gel filtration
74000
-
-
spleen
77000
78000
-
gel filtration
90000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE; 2 * 34000, SDS-PAGE
dimer
-
2 * 31540
dimer
-
2 * 32000, homodimer, SDS-PAGE
dimer
-
2 * 32000, homodimer, SDS-PAGE
dimer
-
2 * 31600, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
dimer
Escherichia coli DH5-alpha
-
2 * 32000, homodimer, SDS-PAGE
-
dimer
Escherichia coli JF611
-
2 * 33000, SDS-PAGE; 2 * 34000, SDS-PAGE
-
dimer
Escherichia coli SO268
-
2 * 31540
-
dimer
Escherichia coli SO5201
-
2 * 32000, homodimer, SDS-PAGE
-
dimer
Nocardioides sp. CT16
-
2 * 18000, SDS-PAGE
-
homotetramer
C0IL37, -
4 * 16600, calculated from amino acid sequence; 4 * 20000, SDS-PAGE
homotetramer
P32320
4 * 15000, SDS-PAGE
homotetramer
-
4 * 14000, SDS-PAGE
homotetramer
-
4 * 13938, electrospray ionization mass spectrometry; 4 * 14000, SDS-PAGE; 4 * 14072, calculated from amino acid sequence
homotetramer
Bacillus caldolyticus DSM405 (T53), Geobacillus stearothermophilus IFO12550 (T101)
-
4 * 14000, SDS-PAGE
-
monomer
-
1 * 54000
tetramer
-
4 * 14000, deduced from cdd structural gene nucleotide sequence and mini-cell experiments
tetramer
-
-
tetramer
-
4 * 13500, SDS-PAGE
tetramer
-
4 * 15000, SDS-PAGE, purified enzyme, homotetramer; 4 * 16000, amino acid sequence
tetramer
-
4 * 14800
tetramer
-
4 * 15000
tetramer
-
-
tetramer
-, Q9R2S1
4 * 14237, calculation from nucleotide sequence; 4 * 15000, SDS-PAGE
tetramer
Q9S3M0, -
4 * 14600, calculation from nucleotide sequence; 4 * 15000, SDS-PAGE
tetramer
P56389
homotetramer
tetramer
-
4 * 15000, SDS-PAGE
tetramer
-
homotetramer, residue Y33 is involved in enzyme folding, enzyme structure analysis using circular dichroism, molecular modeling, overview
monomer
Escherichia coli Y-70-272
-
1 * 54000
-
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
additional information
-
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt
additional information
-
APOBEC3G cytidine deaminase catalytically inactive N-terminal CD1 domain has a predicted large net positive charge, in contrast to the catalytically active CD2 domain, and is likely to govern the mobility of APOBEC3G cytidine deaminase on ssDNA, which should depend on metal ion concentration
additional information
-
A3G contains two cytidine deaminase domains. The CD2 domain possesses the deamination activity
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of tetrameric cytidine deaminase at 2.0 A resolution, hanging drop vapour-diffusion method
-
hanging drop vapour diffusion method. R56A and R56Q crystallize in the same space group as the wild-type enzyme with two subunits in the asymmetric unit, whereas C53H/R56Q can not crystallize in this crystal form but is crystallized in another space group, P3(2)21, with a full tetramer in the asymmetric unit
-
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
-
in complex with tetrahydrouridine, 3-deazauridine, or cytidine. Two alternate conformations of R68 influence zinc-product interaction; purified recombinant CDA complexed with either tetrahydrouridine, 3-deazauridine, or cytidine, hanging drop vapor diffusion technique, 25C, protein solution, containing 10-15 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 1 mM DTT, and 5 mM ligand, is mixed with crystallization solution containing 2.0 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, crystals appear after a few hours or several days, respectively, X-ray diffraction structure determination and analysis at 1.48-2.36 A resolutions, molecular replacement
P56389
hanging drop vapor diffusion method
-
purified CDA in complex with uridine and deoxyuridine, hanging drop vapor diffusion method, 0.002 ml of 12 mg/ml protein in 20 mM Tris-HCl pH 7.5 is mixed with 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.5 and 4.3 M sodium chloride, ligands uridine and deoxyuridine are added by soaking method, X-ray diffractiuon structure determination and analysis at 2.4 and 1.9 A resolution,molecular dynamics simulation, structure modeling
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
10.5
-
deoxycytidine as substrate, beyond these extremes rapid inactivation
3.5
10.5
-
deoxycytidine as substrate, beyond these extremes rapid inactivation
5.5
9.5
-
stable for some hours at 4C, rapid inactivation and precipitation of the enzyme occurs at pH lower 5
6
9
-
reasonably stable in this range
6.5
10.7
-
irreversible loss of activity at pH values below 4
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
80
P32320
-
15
75
-
wild-type enzyme and mutant R68Q are stable, while the stability of mutant Y60G is decreased above 65C
50
-
-
relatively heat stable, no loss of activity when heated for 15 min, activity completely lost after heating at 75C
50
-
-
15 min, absence of dithiothreitol, 44% residual activity
60
-
-
relatively labile to thermal treatment, complete inactivation by incubation for 30 min
65
-
-, Q9R2S1
stable up to
70
90
-
the CDA activity of genes SH1067 and SH1077 remains constant for 3 h at 70C, the half-time of residual activities of SH1067 and SH1077 increases up to 200% as compared with that of gene T53 at 80C, SH1067 shows over 200% increased half-time than that of T53, although 120 min later, no activity remains at 90C. SH2426 shows 150% increased half-time than that of T53 at 70C. SH2429 shows over 50-70% decreased thermostability than that of T53 at 70C, residual activity disappears after 10 min at over 80C
72
-
-
30 min, irreversible denaturation
72
-
Q9S3M0, -
30 min, irreversible denaturation
80
-
-
stable for at least 60 min
90
-
-
5 min, 33% loss of activity
100
-
-
15 min, 1 mM dithiothreitol, 80% residual activity; 1 h, 1 mM dithiothreitol, 48% residual activity; 1 h, presence of D,L-lipoic acid, pH 7.0, 75% residual activity; 2 h, 50 mM dithiothreitol, 56% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
irreversible denaturation after 30 min at 72C
-
unstable in air, even in the frozen state, stabilization achieved under anaerobic conditions
-
very unstable
-
irreversible denaturation at 72C after 30 min
Q9S3M0, -
unstable in air, even in the frozen state, stabilization achieved under anaerobic conditions
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% glycerol, very stable, litle loss of enzymatic activity after 1 year
-
-20C, enzyme lost about 50% activity after 24 h, essentially all activity lost after 48 h
-
4C, enzyme lost about 50% activity after 24 h, essentially all activity lost after 48 h
-
-20C, 50 mM phosphate buffer pH7.5 after 1 month pure enzyme retains 70% original activity
-
-20C, 50 mM Tris-HCl, pH7.5, after 1 month pure enzyme retains 80% original activity
-
-20C, preparations kept 4 months retains original activity
-
4C, 50 mM Tris-HCl, pH 7.5, pure enzyme retains 63% original activity after 2 weeks
-
4C, in presence of 5 mM mercaptoethanol, reasonably stable, retains 47% of its activity after 3 months, freezing inactivates the enzyme, less than 30% recovery of activity after 1 freeze-thaw cycle
-
4C, reasonably stable, retains 55% of its activity after 3 weeks
-
4C, stable for several days, may be kept for months without significant loss of activity if frozen
-
4C,50 mM phosphate buffer pH 7.5, pure enzyme retains 13% original activity after 2 weeks
-
-20C, 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
-
-20C, 20% glycerol appears to be necessary to prevent inactivation from occuring after freezing and thawing
-
-20C crude enzyme is stable for 4 weeks, repeated freezing and thawing destroy the activity
-
-20C, 0.005 M dithiothreitol, enzymatic activity is stable for many weeks
-
4C, very unstable, 50% of activity lost on storage for 24 h or 24 h at room temperature
-
-20C, shows no appreciable loss of activity within 1 month
-
4C, stable for some hours at pH 5.5-9.5
-
-20C, enzyme lost about 50% activity after 24 h, no activity remains after 24 h
-
4C, enzyme lost about 50% activity after 24 h, no activity remains after 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA column chromatography
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography
C0IL37, -
DEAE-52 column chromatography, phenyl Sepharose column chromatography, and ultrafiltration
P32320
recombinant enzyme partially from 3T3 NIH and 3T3-CD3-V5 cells by ammonium sulfate fractionation
-
recombinant wild-type and mutant GST-tagged fusion AIDs from insect cells
-
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
-
recombinant enzyme from Escherichia coli strain BL21 by two steps of anion exchange chromatography, and gel filtration
P56389
Q Sepharose column chromatography, Sephacryl S-200 gel filtration, and butyl-Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA coding for AT-CDA1 amplified, subcloned into pTrc99-A, induced and expressed and overproduced in Escherichia coli SO5201
-
gene At-cda1, located on chromosome 2 PCR amplified, cloned and sequenced, expressed in Escherichia coli BL21(D3)
-
expressed in Escherichia coli Rosetta(DE3)pLysS cells
-
expression in Escherichia coli
-, Q9R2S1
cdd genes cloned and characterized
-
overexpression of wild-type enzyme and mutant enzymes R56A, R56Q and C53H/R56Q in Escherichia coli
-
cdd gene cloned and amplified with pTK148, cloning vector pBR322, enzyme overexpression in Escherichia coli C600
-
SO268 harboring plasmid pSO143 containing the B. subtilis cytidine deaminase gene
-
yielding plasmid pAA5970
-
expressed in Escherichia coli Rosetta(DE3)pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
C0IL37, -
cDNA, PCR, vector pTrc99A, cloned and expressed in Escherichia coli DH5alpha
-
expression of activation-induced deaminase, i.e. AID, and APOBEC3G in Escherichia coli strain BW310 and in human HEK293T cells
-
expression of wild-type and mutant AIDs in insect cells as GST-tagged fusion proteins
-
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
-
gene A3DE
-
incorporation of hA3G CD1 and CD2 domain mutants into HIV-1. Cotransfection of plasmids coding HIV-1 vif and plasmids containing either wild-type or mutant hA3G in 293T cells
-
mutant enzyme Y33G is expressed in Escherichia coli SO5201cells
P32320
enzyme expression in Escherichia coli strain BL21
P56389
expression of 3H9 VDJ knock-in alleles in genomic DNA of immature/T1, mature follicular B cells, and thymocytes from 3H9 and 3H9.Aicda-/- mice, quantitative expression analysis by PCR and immunofluorescence
-
expression of activation-induced deaminase, i.e. AID, and APOBEC3G in Escherichia coli strain BW310 and in human HEK293T cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
Q9S3M0, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
significant up-regulation of CDA is observed after lipopolysaccharide (3fold after 18 h) or polyriboinosinic polyribocytidylic acid challenge (4.5fold after 18 h)
C0IL37, -
sorbitol or cyclodextrins does not induce expression of the mutant enzyme Y33G
P32320
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
P32320
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C53H
-
attempts to express and purify the mutant enzyme are unsuccessful
C53H/R56Q
-
mutant enzyme contains the same amount of zinc as the wild-type enzyme. Because of dissociation into its inactive subunits, it is impossible to determine the kinetic parameters for the mutant enzyme
R56A
-
mutant enzyme contains the same amount of zinc as the wild-type enzyme. Similar KM-value but decreased Vmax-value compared to wild-type enzyme
R56D
-
zinc-binding capacity of mutant enzyme is reduced
R56Q
-
mutant enzyme contains the same amount of zinc as the wild-type enzyme. Similar KM-value but decreased Vmax-value compared to wild-type enzyme
A111E
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant; site-directed mutagenesis, the mutation may alter the stability of the specificity loop, leading to the inability of AID to properly position the substrate in the active center
C320A
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320D
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320F
-
site-directed mutagenesis, the mutation poorly recovers the anti-HIV-1 activity of A3DE
C320K
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320L
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320N
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320Q
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320S
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320T
-
site-directed mutagenesis, the mutation fails to recover the anti-HIV-1 activity of A3DE
C320W
-
site-directed mutagenesis, the mutation poorly recovers the anti-HIV-1 activity of A3DE
C320Y
-
site-directed mutagenesis, replacing C320 with a corresponding tyrosine from A3F (Y307) increases A3DE antiviral activity more than 20fold
C332R/K342E
-
site-directed mutagenesis
D314F/Y315W
-
site-directed mutagenesis
F11L
-
site-directed mutagenesis, an inactive HIGM-2 mutant, the mutation may disrupt alpha-helix 1 hydrophobic packing to the structure resulting in destabilization of the AC-Loop 1
F126A/W127A
-
site-directed mutagenesis, the N-terminal CD1 domain mutant, that shows disrupted dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C to U deaminations with 3'-5' deamination polarity, similar to wild-type Apo3G. The mutation causes severe disruption in oligomer formation resulting in about 92% monomers and 8% dimers, with no larger oligomer forms detected
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
F151S
-
site-directed mutagenesis, inactive mutant
F15L
-
site-directed mutagenesis, a HIGM-2 mutant, that shows low residual activity, F15L catalyzes highly processive C deaminations similar to wild-type AID, about 2% of the F15L mutants may retain sufficient structural integrity of the AC-Loop1 to permit an essentially normal deamination pattern the mutation may disrupt alpha-helix 1 hydrophobic packing to the structure resulting in destabilization of the AC-Loop 1; site-directed mutagenesis, inactive mutant
I136K
-
site-directed mutagenesis, inactive mutant
I314A/Y315A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
K320Q/A322G
-
site-directed mutagenesis
K342E
-
site-directed mutagenesis
K342R
-
site-directed mutagenesis
L106P
-
site-directed mutagenesis, inactive mutant
L113P
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant; site-directed mutagenesis, the mutation may alter the stability of the specificity loop, leading to the inability of AID to properly position the substrate in the active center
L221R/C224Y
-
site-directed mutagenesis
L98R
-
site-directed mutagenesis, mutant L98R is 25fold less active than wild-type AID
M139V
-
site-directed mutagenesis, inactive mutant
P317T/L318D
-
site-directed mutagenesis
R112C
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant; site-directed mutagenesis, the mutation may alter the stability of the specificity loop, leading to the inability of AID to properly position the substrate in the active center
R174S
-
site-directed mutagenesis, mutant R174S is 200fold less active than wild-type AID. R174S binds to ssDNA weakly, but cooperatively
R24W
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant
R313A/D316A/D317A/Q318A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
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
S43P
-
site-directed mutagenesis, mutant S43P shows about 30% of wild-type AID activity
S83P
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant
S85N
-
site-directed mutagenesis, substrate interaction mutant, inactive mutant
T238V/A243P/F245S/R246W
-
site-directed mutagenesis
V350K/S351Y/K354E/S359N
-
site-directed mutagenesis
W80R
-
site-directed mutagenesis, inactive mutant
Y124A/Y125A
-
site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa
Y307A
-
site-directed mutagenesis, the mutation disrupts A3F anti-HIV-1 activity
Y307C
-
site-directed mutagenesis, the mutation disrupts A3F anti-HIV-1 activity
Y307K
-
site-directed mutagenesis, the mutation disrupts A3F anti-HIV-1 activity
Y307R
-
site-directed mutagenesis, the mutation disrupts A3F anti-HIV-1 activity
Y33F
-
site-directed mutagenesis, inactive monomeric enzyme
Y33G
-
site-directed mutagenesis, inactive monomeric enzyme
Y33G
P32320
the mutant shows severely decreased Km values compared to the wild type enzyme. Deoxycytidine is the best substrate for Y33G, while cytosine arabinoside is not substrate. Y33G is a thermolabile enzyme with an optimal temperature around 40C, while above 60C it is completely inactivated in an irreversible manner
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
T218A
-
site-directed mutagenesis
T218E
-
site-directed mutagenesis
T27A
-
site-directed mutagenesis
T27E
-
site-directed mutagenesis
M6T
-
site-directed mutagenesis, an inactive HIGM-2 mutant, the mutation may disrupt alpha-helix 1 hydrophobic packing to the structure resulting in destabilization of the AC-Loop 1
additional information
-
comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview
additional information
-
phospho-mimetic mutations inhibit DNA cytidine deaminase activity
additional information
-
identification of mutations involved in the HIGM-2 syndrome, the twenty-three missense mutations identified in humans span almost the entire gene for AID resulting in a recessive phenotype. Construction of a series of point mutants and of C-terminal deletion mutants, giving mutant class IV, that retain catalytic activity and processivity for deletions up to C18, with DELTAC10 and DELTAC15 having 2 to 3fold higher specific activities than wild-type enzyme. Deleting nineteen C-terminal amino acids inactivates AID
additional information
-
construction of three A3DE chimeric mutants. The A3B+F chimera contains the A3B N-terminal domain and A3F C-terminal domain, and A3B+DE and A3DE+F chimeras contain other combinations of the N-terminal and C-terminal domains from A3B, A3DE, or A3F. Both A3B+DeFF and A3B+FFDe proteins lack the A3DE region II. C320 deletion mutant, C320DELTA, and a LCYFWI-YDD mutant that has the LCYFW subdomain replaced with a corresponding A3G IYDD subdomain. Both mutations fail to increase the anti-HIV activity of A3DE
additional information
-
CD2-2, possessing the deamination activity, incorporated efficiently into HIV-1 is unable to mutate viral cDNA. Construction of three A3G mutants CD1-1, CD2-2 and CD2-1, which contain duplicate CD1 domain, duplicate CD2 domain, and position switched CD domain, respectively. The two CD domains are functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif of hA3G, whereas CD domain switch or replacement greatly affect the sensitivity to Vif-induced degradation, editing and antiviral activity of hA3G. The switch of the CD domain affects nucleotide sequence preference pattern of the deaminase. The mutants show a nucleotide sequence preference pattern
E259Q
-
site-directed mutagenesis
additional information
-
phospho-mimetic mutations inhibit DNA cytidine deaminase activity
additional information
-
generation of several enzyme-deficient Aicda-/- mice
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after partial denaturation at 72C for 30 min and following renaturation on ice, the enzyme retains its enzymatic activity
-, Q9R2S1
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
activation and inactivation of several deoxycytidine antimetabolites
medicine
-
different effect of cytidine in blood cells from healthy donors and chronic lymphocytic and acute myeloblastic leukemia patients
medicine
-
enzyme limits the effectiveness of the antineoplastic agent cytosine arabinoside or aracytidine in the treatment of acute myeloblastic leukemias, chemotherapeutic use of the inhibitor THU to protect antileukemic agents from deaminase attack, inhibitors of cytidine deaminase prolongs the plasma halflife of antitumor or antiviral drugs
medicine
-
-
medicine
-
studies on radiosensitization of glioblastoma multiforme (GBM), deoxynucleoside analogue gemcitabine (dFdC) considered for combination therapy with radiation in glioblastomas
drug development
-
CDA is a target for development of specific enzyme inhibitors with potential anti-proliferative activity on cell growth of Mycobacterium tuberculosis, the major causative agent of tuberculosis