Cytidine deaminase

CDA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1MQ0
Identifiers
Aliases	CDA, CDD, cytidine deaminase
External IDs	OMIM: 123920 MGI: 1919519 HomoloGene: 1352 GeneCards: CDA
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	20,618,903 bp[1]
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)[2]
End	138,095,303 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; blood; ; bone marrow; ; right lobe of liver; ; cancellous bone; ; bone marrow cells; ; rectum; ; gums; ; spleen; ; skin of abdomen;
	Top expressed in
	duodenum; ; kidney; ; intestinal villus; ; jejunum; ; proximal tubule; ; facial motor nucleus; ; islet of Langerhans; ; placenta; ; yolk sac; ; left lobe of liver;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein homodimerization activity; nucleoside binding; cytidine deaminase activity; zinc ion binding; metal ion binding; protein binding; catalytic activity; identical protein binding; hydrolase activity;
Cellular component	cytosol; extracellular region; secretory granule lumen; tertiary granule lumen; ficolin-1-rich granule lumen;
Biological process	cytosine metabolic process; pyrimidine nucleoside salvage; cell surface receptor signaling pathway; cytidine deamination; negative regulation of cell growth; pyrimidine-containing compound salvage; negative regulation of nucleotide metabolic process; protein homotetramerization; neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	978
	72269
	ENSG00000158825
	ENSMUSG00000028755
	P32320
	P56389
	NM_001785
	NM_028176
	NP_001776
	NP_082452
	Wikidata
View/Edit Human	View/Edit Mouse

Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.[5][6][7]

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.[7] Most cytidine deaminases act on RNA, and the few that act on DNA require ssDNA.[8]

A related activation-induced (cytidine) deaminase (AID) regulates antibody diversification, especially the process of somatic hypermutation.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

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|alt=Fluorouracil (5-FU) Activity edit]]

Fluorouracil (5-FU) Activity edit

The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

References

GRCh38: Ensembl release 89: ENSG00000158825 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000028755 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Kühn K, Bertling WM, Emmrich F (January 1993). "Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation". Biochemical and Biophysical Research Communications. 190 (1): 1–7. doi:10.1006/bbrc.1993.1001. PMID 8422236.
Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E (December 1998). "Isolation and characterization of the gene coding for human cytidine deaminase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1443 (3): 323–33. doi:10.1016/s0167-4781(98)00235-8. PMID 9878810.
"Entrez Gene: CDA cytidine deaminase".
Komor AC, Kim YB, Packer MS, Zuris JA, Liu DR (May 2016). "Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage". Nature. 533 (7603): 420–4. Bibcode:2016Natur.533..420K. doi:10.1038/nature17946. PMC 4873371. PMID 27096365.

Wentworth DF, Wolfenden R (November 1975). "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 (October 1994). "Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA". Cancer Research. 54 (20): 5401–7. PMID 7923172.
Saccone S, Besati C, Andreozzi L, Della Valle G, Garattini E, Terao M (August 1994). "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, Løvhaug D, Seeberg EC (June 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. doi:10.1182/blood.V91.11.4127. PMID 9596658.
Somasekaram A, Jarmuz A, How A, Scott J, Navaratnam N (October 1999). "Intracellular localization of human cytidine deaminase. Identification of a functional nuclear localization signal". The Journal of Biological Chemistry. 274 (40): 28405–12. doi:10.1074/jbc.274.40.28405. PMID 10497201.
Wistow G, Bernstein SL, Wyatt MK, Behal A, Touchman JW, Bouffard G, et al. (June 2002). "Expressed sequence tag analysis of adult human lens for the NEIBank Project: over 2000 non-redundant transcripts, novel genes and splice variants". Molecular Vision. 8: 171–84. PMID 12107413.
Taysi S, Polat MF, Sari RA, Bakan E (May 2002). "Serum adenosine deaminase and cytidine deaminase activities in patients with systemic lupus erythematosus". Clinical Chemistry and Laboratory Medicine. 40 (5): 493–5. doi:10.1515/CCLM.2002.085. PMID 12113294. S2CID 32965037.
Bransteitter R, Pham P, Scharff MD, Goodman MF (April 2003). "Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase". Proceedings of the National Academy of Sciences of the United States of America. 100 (7): 4102–7. Bibcode:2003PNAS..100.4102B. doi:10.1073/pnas.0730835100. PMC 153055. PMID 12651944.
Sun ZQ, Jiang B, Zhao XS, Bao L, Wu T, Lu XJ, et al. (June 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, Mariani P, Quadrini B, Cammertoni N, Vita A (2003). "Intersubunit interactions in human cytidine deaminase". Nucleosides, Nucleotides & Nucleic Acids. 22 (5–8): 1535–8. doi:10.1081/NCN-120023028. PMID 14565460. S2CID 8626156.
Costanzi S, Vincenzetti S, Vita A, Lambertucci C, Taffi S, Volpini R, 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. S2CID 6849333.
Ge Y, Jensen TL, Stout ML, Flatley RM, Grohar PJ, Ravindranath Y, et al. (January 2004). "The role of cytidine deaminase and GATA1 mutations in the increased cytosine arabinoside sensitivity of Down syndrome myeloblasts and leukemia cell lines". Cancer Research. 64 (2): 728–35. doi:10.1158/0008-5472.CAN-03-2456. PMID 14744791.
Vincenzetti S, De Sanctis G, Costanzi S, Cristalli G, Mariani P, Mei G, et al. (December 2003). "Functional properties of subunit interactions in human cytidine deaminase". Protein Engineering. 16 (12): 1055–61. doi:10.1093/protein/gzg117. PMID 14983087.
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, et al. (October 2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Chung SJ, Fromme JC, Verdine GL (February 2005). "Structure of human cytidine deaminase bound to a potent inhibitor". Journal of Medicinal Chemistry. 48 (3): 658–60. doi:10.1021/jm0496279. PMID 15689149.
Vincenzetti S, Mariani PL, Cammertoni N, Polzonetti V, Natalini P, Quadrini B, et al. (December 2004). "Isoenzymatic forms of human cytidine deaminase". Protein Engineering, Design & Selection. 17 (12): 871–7. doi:10.1093/protein/gzh101. PMID 15713780.
Costanzi S, Vincenzetti S, Cristalli G, Vita A (September 2006). "Human cytidine deaminase: a three-dimensional homology model of a tetrameric metallo-enzyme inferred from the crystal structure of a distantly related dimeric homologue". Journal of Molecular Graphics & Modelling. 25 (1): 10–6. doi:10.1016/j.jmgm.2005.10.008. PMID 16303324.

External links

Overview of all the structural information available in the PDB for UniProt: P32320 (Cytidine deaminase) at the PDBe-KB.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[WikiPathways-9] The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000158825 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028755 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8422236-5] Kühn K, Bertling WM, Emmrich F (January 1993). "Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation". Biochemical and Biophysical Research Communications. 190 (1): 1–7. doi:10.1006/bbrc.1993.1001. PMID 8422236.

[pmid9878810-6] Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E (December 1998). "Isolation and characterization of the gene coding for human cytidine deaminase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1443 (3): 323–33. doi:10.1016/s0167-4781(98)00235-8. PMID 9878810.

[entrez-7] "Entrez Gene: CDA cytidine deaminase".

[8] Komor AC, Kim YB, Packer MS, Zuris JA, Liu DR (May 2016). "Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage". Nature. 533 (7603): 420–4. Bibcode:2016Natur.533..420K. doi:10.1038/nature17946. PMC 4873371. PMID 27096365.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Cytidine deaminase

Interactive pathway map

References

Further reading

External links