Cytidine deaminase: Difference between revisions
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'''Cytidine deaminase''' is an [[enzyme]] that in humans is encoded by the ''CDA'' [[gene]].<ref name="pmid8422236">{{cite journal | vauthors = Kuhn K, Bertling WM, Emmrich F | title = Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation | journal = Biochem Biophys Res Commun | volume = 190 | issue = 1 | pages = 1–7 |date=Feb 1993 | pmid = 8422236 | pmc = | doi = 10.1006/bbrc.1993.1001 }}</ref><ref name="pmid9878810">{{cite journal | vauthors = Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E | title = Isolation and characterization of the gene coding for human cytidine deaminase | journal = Biochim Biophys Acta | volume = 1443 | issue = 3 | pages = 323–33 |date=Feb 1999 | pmid = 9878810 | pmc = | doi = 10.1016/s0167-4781(98)00235-8}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CDA cytidine deaminase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=978| accessdate = }}</ref> | |||
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| section_title = | |||
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CDA cytidine deaminase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=978| accessdate = }}</ref> | |||
}} | |||
A related [[activation-induced (cytidine) deaminase]] (AID) regulates [[antibody]] diversification, especially the process of [[somatic hypermutation]]. | |||
== Interactive pathway map == | |||
{{FluoropyrimidineActivity WP1601|highlight=Cytidine_deaminase}} | |||
==References== | |||
{{reflist}} | |||
==Further reading== | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{cite journal | vauthors=Wentworth DF, Wolfenden R |title=On the interaction of 3,4,5,6-tetrahydrouridine with human liver cytidine deaminase. |journal=Biochemistry |volume=14 |issue= 23 |pages= 5099–105 |year= 1976 |pmid= 53069 |doi=10.1021/bi00694a012 }} | |||
*{{cite journal | vauthors=Laliberté J, Momparler RL |title=Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA. |journal=Cancer Res. |volume=54 |issue= 20 |pages= 5401–7 |year= 1994 |pmid= 7923172 |doi= }} | |||
*{{cite journal | vauthors=Saccone S, Besati C, Andreozzi L |title=Assignment of the human cytidine deaminase (CDA) gene to chromosome 1 band p35-p36.2. |journal=Genomics |volume=22 |issue= 3 |pages= 661–2 |year= 1995 |pmid= 8001985 |doi= 10.1006/geno.1994.1448 |display-authors=etal}} | |||
*{{cite journal | vauthors=Gran C, Bøyum A, Johansen RF |title=Growth inhibition of granulocyte-macrophage colony-forming cells by human cytidine deaminase requires the catalytic function of the protein. |journal=Blood |volume=91 |issue= 11 |pages= 4127–35 |year= 1998 |pmid= 9596658 |doi= |display-authors=etal}} | |||
*{{cite journal | vauthors=Somasekaram A, Jarmuz A, How A |title=Intracellular localization of human cytidine deaminase. Identification of a functional nuclear localization signal. |journal=J. Biol. Chem. |volume=274 |issue= 40 |pages= 28405–12 |year= 1999 |pmid= 10497201 |doi=10.1074/jbc.274.40.28405 |display-authors=etal}} | |||
*{{cite journal | vauthors=Wistow G, Bernstein SL, Wyatt MK |title=Expressed sequence tag analysis of adult human lens for the NEIBank Project: over 2000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue= |pages= 171–84 |year= 2002 |pmid= 12107413 |doi= |display-authors=etal}} | |||
*{{cite journal | vauthors=Taysi S, Polat MF, Sari RA, Bakan E |title=Serum adenosine deaminase and cytidine deaminase activities in patients with systemic lupus erythematosus. |journal=Clin. Chem. Lab. Med. |volume=40 |issue= 5 |pages= 493–5 |year= 2003 |pmid= 12113294 |doi=10.1515/CCLM.2002.085 }} | |||
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | |||
*{{cite journal | vauthors=Bransteitter R, Pham P, Scharff MD, Goodman MF |title=Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 7 |pages= 4102–7 |year= 2003 |pmid= 12651944 |doi= 10.1073/pnas.0730835100 | pmc=153055 }} | |||
*{{cite journal | vauthors=Sun ZQ, Jiang B, Zhao XS |title=[Expression of cytidine deaminase mRNA in bone marrow cells from patients with acute leukemia] |journal=Zhongguo Shi Yan Xue Ye Xue Za Zhi |volume=11 |issue= 3 |pages= 246–50 |year= 2003 |pmid= 12844405 |doi= |display-authors=etal}} | |||
*{{cite journal | vauthors=Vincenzetti S, Costanzi S, Cristalli G |title=Intersubunit interactions in human cytidine deaminase. |journal=Nucleosides Nucleotides Nucleic Acids |volume=22 |issue= 5-8 |pages= 1535–8 |year= 2003 |pmid= 14565460 |doi=10.1081/NCN-120023028 |display-authors=etal}} | |||
*{{cite journal | vauthors=Costanzi S, Vincenzetti S, Vita A |title=Human cytidine deaminase: understanding the catalytic mechanism. |journal=Nucleosides Nucleotides Nucleic Acids |volume=22 |issue= 5-8 |pages= 1539–43 |year= 2003 |pmid= 14565461 |doi=10.1081/NCN-120023029 |display-authors=etal}} | |||
*{{cite journal | vauthors=Ge Y, Jensen TL, Stout ML |title=The role of cytidine deaminase and GATA1 mutations in the increased cytosine arabinoside sensitivity of Down syndrome myeloblasts and leukemia cell lines. |journal=Cancer Res. |volume=64 |issue= 2 |pages= 728–35 |year= 2004 |pmid= 14744791 |doi=10.1158/0008-5472.CAN-03-2456 |display-authors=etal}} | |||
*{{cite journal | vauthors=Vincenzetti S, De Sanctis G, Costanzi S |title=Functional properties of subunit interactions in human cytidine deaminase. |journal=Protein Eng. |volume=16 |issue= 12 |pages= 1055–61 |year= 2004 |pmid= 14983087 |doi= 10.1093/protein/gzg117 |display-authors=etal}} | |||
*{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | |||
*{{cite journal | vauthors=Chung SJ, Fromme JC, Verdine GL |title=Structure of human cytidine deaminase bound to a potent inhibitor. |journal=J. Med. Chem. |volume=48 |issue= 3 |pages= 658–60 |year= 2005 |pmid= 15689149 |doi= 10.1021/jm0496279 }} | |||
*{{cite journal | vauthors=Vincenzetti S, Mariani PL, Cammertoni N |title=Isoenzymatic forms of human cytidine deaminase. |journal=Protein Eng. Des. Sel. |volume=17 |issue= 12 |pages= 871–7 |year= 2005 |pmid= 15713780 |doi= 10.1093/protein/gzh101 |display-authors=etal}} | |||
*{{cite journal | vauthors=Costanzi S, Vincenzetti S, Cristalli G, Vita A |title=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=J. Mol. Graph. Model. |volume=25 |issue= 1 |pages= 10–6 |year= 2007 |pmid= 16303324 |doi= 10.1016/j.jmgm.2005.10.008 }} | |||
}} | |||
{{refend}} | |||
{{PDB Gallery|geneid=978}} | |||
{{Carbon-nitrogen non-peptide hydrolases}} | |||
{{Enzymes}} | |||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
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[[Category:EC 3.5.4]] | |||
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Latest revision as of 20:31, 30 July 2018
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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]
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]
Fluorouracil (5-FU) Activity edit
- ↑ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".
References
- ↑ 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.
- ↑ 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. doi:10.1016/s0167-4781(98)00235-8. PMID 9878810.
- ↑ 3.0 3.1 "Entrez Gene: CDA cytidine deaminase".
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.
- 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.
- 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.
- 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.
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