Cytidine deaminase

Cytidine deaminase
PDB rendering based on 1mq0.
Available structures PDB 1mq0
Identifiers
Symbols	CDA; CDD
External IDs	OMIM: 123920 MGI: 1919519 HomoloGene: 1352 GeneCards: CDA Gene
EC number	3.5.4.5
Gene Ontology Molecular function • nucleoside binding • cytidine deaminase activity • cytidine deaminase activity • zinc ion binding • zinc ion binding • hydrolase activity • protein homodimerization activity • metal ion binding Cellular component • extracellular region • cytosol • cytosol Biological process • pyrimidine base metabolic process • cell surface receptor linked signaling pathway • pyrimidine-containing compound salvage • cytidine deamination • cytidine deamination • cytosine metabolic process • negative regulation of cell growth • pyrimidine nucleoside salvage • negative regulation of nucleotide metabolic process • protein homotetramerization • nucleobase, nucleoside and nucleotide metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	978	72269
Ensembl	ENSG00000158825	ENSMUSG00000028755
UniProt	P32320	Q8R219
RefSeq (mRNA)	NM_001785	NM_028176.1
RefSeq (protein)	NP_001776	NP_082452.1
Location (UCSC)	Chr 1: 20.92 – 20.95 Mb	Chr 4: 137.89 – 137.92 Mb
PubMed search	[1]	[2]

Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.^[1][2][3]

This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool. Mutations in this gene are associated with decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.^[3]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective Wikipedia articles. ^[4]

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Fluorouracil (5-FU) Activity edit

References

1. ^ Kuhn K, Bertling WM, Emmrich F (Feb 1993). "Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation". Biochem Biophys Res Commun 190 (1): 1–7. doi:10.1006/bbrc.1993.1001. PMID 8422236. 
2. ^ Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E (Feb 1999). "Isolation and characterization of the gene coding for human cytidine deaminase". Biochim Biophys Acta 1443 (3): 323–33. PMID 9878810. 
3. ^ ^{a b} "Entrez Gene: CDA cytidine deaminase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=978. 
4. ^ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601". http://www.wikipathways.org/index.php/Pathway:WP1601. 

Further reading

• Wentworth DF, Wolfenden R (1976). "On the interaction of 3,4,5,6-tetrahydrouridine with human liver cytidine deaminase.". Biochemistry 14 (23): 5099–105. doi:10.1021/bi00694a012. PMID 53069. 
• Laliberté J, Momparler RL (1994). "Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA.". Cancer Res. 54 (20): 5401–7. PMID 7923172. 
• Saccone S, Besati C, Andreozzi L, et al. (1995). "Assignment of the human cytidine deaminase (CDA) gene to chromosome 1 band p35-p36.2.". Genomics 22 (3): 661–2. doi:10.1006/geno.1994.1448. PMID 8001985. 
• Gran C, Bøyum A, Johansen RF, et al. (1998). "Growth inhibition of granulocyte-macrophage colony-forming cells by human cytidine deaminase requires the catalytic function of the protein.". Blood 91 (11): 4127–35. PMID 9596658. 
• Somasekaram A, Jarmuz A, How A, et al. (1999). "Intracellular localization of human cytidine deaminase. Identification of a functional nuclear localization signal.". J. Biol. Chem. 274 (40): 28405–12. doi:10.1074/jbc.274.40.28405. PMID 10497201. 
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of adult human lens for the NEIBank Project: over 2000 non-redundant transcripts, novel genes and splice variants.". Mol. Vis. 8: 171–84. PMID 12107413. 
• Taysi S, Polat MF, Sari RA, Bakan E (2003). "Serum adenosine deaminase and cytidine deaminase activities in patients with systemic lupus erythematosus.". Clin. Chem. Lab. Med. 40 (5): 493–5. doi:10.1515/CCLM.2002.085. PMID 12113294. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Bransteitter R, Pham P, Scharff MD, Goodman MF (2003). "Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase.". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 4102–7. doi:10.1073/pnas.0730835100. PMC 153055. PMID 12651944. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=153055. 
• Sun ZQ, Jiang B, Zhao XS, et al. (2003). "[Expression of cytidine deaminase mRNA in bone marrow cells from patients with acute leukemia]". Zhongguo Shi Yan Xue Ye Xue Za Zhi 11 (3): 246–50. PMID 12844405. 
• Vincenzetti S, Costanzi S, Cristalli G, et al. (2003). "Intersubunit interactions in human cytidine deaminase.". Nucleosides Nucleotides Nucleic Acids 22 (5-8): 1535–8. doi:10.1081/NCN-120023028. PMID 14565460. 
• Costanzi S, Vincenzetti S, Vita A, et al. (2003). "Human cytidine deaminase: understanding the catalytic mechanism.". Nucleosides Nucleotides Nucleic Acids 22 (5-8): 1539–43. doi:10.1081/NCN-120023029. PMID 14565461. 
• Ge Y, Jensen TL, Stout ML, et al. (2004). "The role of cytidine deaminase and GATA1 mutations in the increased cytosine arabinoside sensitivity of Down syndrome myeloblasts and leukemia cell lines.". Cancer Res. 64 (2): 728–35. doi:10.1158/0008-5472.CAN-03-2456. PMID 14744791. 
• Vincenzetti S, De Sanctis G, Costanzi S, et al. (2004). "Functional properties of subunit interactions in human cytidine deaminase.". Protein Eng. 16 (12): 1055–61. doi:10.1093/protein/gzg117. PMID 14983087. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Chung SJ, Fromme JC, Verdine GL (2005). "Structure of human cytidine deaminase bound to a potent inhibitor.". J. Med. Chem. 48 (3): 658–60. doi:10.1021/jm0496279. PMID 15689149. 
• Vincenzetti S, Mariani PL, Cammertoni N, et al. (2005). "Isoenzymatic forms of human cytidine deaminase.". Protein Eng. Des. Sel. 17 (12): 871–7. doi:10.1093/protein/gzh101. PMID 15713780. 
• Costanzi S, Vincenzetti S, Cristalli G, Vita A (2007). "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 (1): 10–6. doi:10.1016/j.jmgm.2005.10.008. PMID 16303324.