3.5.4.14: deoxycytidine deaminase
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For detailed information about deoxycytidine deaminase, go to the full flat file.
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General Information on EC 3.5.4.14 - deoxycytidine deaminase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
AID exhibits strong homology with the catalytically active CD2 domain of Apo3G
evolution
-
an active-site Thr/Ser is conserved in mammalian DNA cytidine deaminases, overview
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
-
the HIGM-2 syndrome results from mutations spanning activation-induced deoxycytidine deaminase, AID. In HIGM-2 syndrome immunoglobulin class-switch recombination is abolished, causing an accumulation of IgM and absence of IgG, IgA and IgE isotypes. Identification of four structural classes of mutants, and contributions of each of the mutants to catalysis/class I, AID-DNA substrate interactions/class II, structural integrity/class III, and C-terminal deletions/class IV,overview
physiological function
-
Apo3G triggers HIV viral inactivation by processively deaminating C->U, with 3->5 polarity, on nascent minus-strand cDNA
physiological function
-
APOBEC3G is a single-stranded DNA cytosine deaminase that eliminates HIV-1 infectivity by converting C to U in numerous small target motifs on the minus viral cDNA. APOBEC3G cytidine deaminase deaminates linear ssDNA in vitro with pronounced spatial asymmetry favoring the 3' to 5' direction. A similar polarity observed in vivo is believed responsible for initiating localized C to T mutational gradients that inactivate the virus
physiological function
-
APOBEC3G is a single-stranded DNA-dependent deoxycytidine deaminase, which, in the absence of the human immunodeficiency virus (HIV) viral infectivity factor, is encapsulated into HIV virions. Subsequently, Apo3G triggers viral inactivation by processively deaminating C to U, with 3'-5' polarity, on nascent minus-strand cDNA
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
additional information
-
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. The CD1 domain is essential for both processivity and polarity, structure modelling, overview
additional information
-
mechanistic studies on ssDNA scanning enzymes, investigation of ssDNA scanning and motif-targeting mechanisms for APOBEC3G cytidine deaminase using single molecule Förster resonance energy transfer, overview
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General Information on EC 3.5.4.14 - deoxycytidine deaminase
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
AID exhibits strong homology with the catalytically active CD2 domain of Apo3G
evolution
-
an active-site Thr/Ser is conserved in mammalian DNA cytidine deaminases, overview
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
-
the HIGM-2 syndrome results from mutations spanning activation-induced deoxycytidine deaminase, AID. In HIGM-2 syndrome immunoglobulin class-switch recombination is abolished, causing an accumulation of IgM and absence of IgG, IgA and IgE isotypes. Identification of four structural classes of mutants, and contributions of each of the mutants to catalysis/class I, AID-DNA substrate interactions/class II, structural integrity/class III, and C-terminal deletions/class IV,overview
physiological function
-
Apo3G triggers HIV viral inactivation by processively deaminating C->U, with 3->5 polarity, on nascent minus-strand cDNA
physiological function
-
APOBEC3G is a single-stranded DNA cytosine deaminase that eliminates HIV-1 infectivity by converting C to U in numerous small target motifs on the minus viral cDNA. APOBEC3G cytidine deaminase deaminates linear ssDNA in vitro with pronounced spatial asymmetry favoring the 3' to 5' direction. A similar polarity observed in vivo is believed responsible for initiating localized C to T mutational gradients that inactivate the virus
physiological function
-
APOBEC3G is a single-stranded DNA-dependent deoxycytidine deaminase, which, in the absence of the human immunodeficiency virus (HIV) viral infectivity factor, is encapsulated into HIV virions. Subsequently, Apo3G triggers viral inactivation by processively deaminating C to U, with 3'-5' polarity, on nascent minus-strand cDNA
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
additional information
-
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. The CD1 domain is essential for both processivity and polarity, structure modelling, overview
additional information
-
mechanistic studies on ssDNA scanning enzymes, investigation of ssDNA scanning and motif-targeting mechanisms for APOBEC3G cytidine deaminase using single molecule Förster resonance energy transfer, overview
