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| {{enzyme
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| | Name = cytosine deaminase
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| | EC_number = 3.5.4.1
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| | CAS_number = 9025-05-2
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| | IUBMB_EC_number = 3/5/4/1
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| | GO_code = 0004131
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| In [[enzymology]], a '''cytosine deaminase''' ({{EC number|3.5.4.1}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :cytosine + H<sub>2</sub>O <math>\rightleftharpoons</math> uracil + NH<sub>3</sub> | |
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[cytosine]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[uracil]] and [[ammonia|NH<sub>3</sub>]].
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| This enzyme belongs to the family of [[hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is '''cytosine aminohydrolase'''. This enzyme is also called '''isocytosine deaminase'''. This enzyme participates in [[pyrimidine metabolism]].
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| ==Structural studies==
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| As of late 2007, 13 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1K6W}}, {{PDB link|1K70}}, {{PDB link|1OX7}}, {{PDB link|1P6O}}, {{PDB link|1R9X}}, {{PDB link|1R9Y}}, {{PDB link|1RA0}}, {{PDB link|1RA5}}, {{PDB link|1RAK}}, {{PDB link|1RB7}}, {{PDB link|1UAQ}}, {{PDB link|1YSB}}, and {{PDB link|1YSD}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = COHEN SS, BARNER HD | date = 1957 | title = The conversion of 5-methyldeoxycytidine to thymidine in vitro and in vivo | journal = J. Biol. Chem. | volume = 226 | pages = 631–42 | pmid = 13438848 | issue = 2 }}
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| * {{cite journal | author = Kream J and Chargaff E | date = 1952 | title = On the cytosine deaminase of yeast | journal = J. Am. Chem. Soc. | volume = 74 | issue = 20 | pages = 5157–5160 | doi = 10.1021/ja01140a050 }}
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| {{hydrolase-stub}}
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| [[Category:EC 3.5.4]]
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| [[Category:Enzymes of known structure]]
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