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3.5.4.5: cytidine deaminase

This is an abbreviated version!
For detailed information about cytidine deaminase, go to the full flat file.

Word Map on EC 3.5.4.5

Reaction

2'-deoxycytidine
+
H2O
=
2'-deoxyuridine
+
NH3

Synonyms

activation-induced cytidine deaminase, AICDA, canine hepatic cyd deaminase, CDA, CDABcald, CDABpsy, CDABsub, CDase, CDD, CR deaminase, cyd deaminase, Cytidine aminohydrolase, cytidine deaminase, cytidine/2'-deoxycytidine aminohydrolase, cytosine nucleoside deaminase, DCD, dCDA, deoxycytidine deaminase, EC 3.5.4.14, mammalian deminase, T-CDA, yeast cytidine deaminase

ECTree

     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

Engineering

Engineering on EC 3.5.4.5 - cytidine deaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
E47A
mutant protein is insoluble
E47D
37fold decrease in kcat value. No kcat and kcat/KM dependence on pH values ranging from 4.0 to 11 is observed
E47H
mutant protein is insoluble
E47L
complete loss of activity
E47Q
19fold decrease in kcat value
E47A
-
mutant protein is insoluble
-
E47D
-
37fold decrease in kcat value. No kcat and kcat/KM dependence on pH values ranging from 4.0 to 11 is observed
-
E47H
-
mutant protein is insoluble
-
E47L
-
complete loss of activity
-
E47Q
-
19fold decrease in kcat value
-