Carnitinamidase: Difference between revisions

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m Robot: Change redirected category EC 3.5.1 to Hydrolases acting on nonpeptide C-N bonds
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m Bot: Change redirected category Hydrolases acting on nonpeptide C-N bonds to EC 3.5.1
 
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{{enzyme
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| Name = cyanuric acid amidohydrolase
| EC_number = 3.5.2.15
| CAS_number = 100785-00-0
| IUBMB_EC_number = 3/5/2/15
| GO_code = 0018753
| image =
| width =
| caption =
}}
In [[enzymology]], a '''cyanuric acid amidohydrolase''' ({{EC number|3.5.2.15}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:cyanuric acid + H<sub>2</sub>O <math>\rightleftharpoons</math> biuret + CO<sub>2</sub>
 
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[cyanuric acid]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[biuret]] and [[carbon dioxide|CO<sub>2</sub>]].
 
This enzyme belongs to the family of [[hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is '''cyanuric acid amidohydrolase'''. This enzyme participates in [[atrazine degradation]].
 
==References==
{{reflist|1}}
* {{cite journal | author = Eaton RW, Karns JS | date = 1991 | title = Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains | journal = J. Bacteriol. | volume = 173 | pages = 1363&ndash;6  | pmid = 1991731 | issue = 3 | pmc = 207267 }}
* {{cite journal | author = Eaton RW, Karns JS | date = 1991 | title = Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227 | journal = J. Bacteriol. | volume = 173 | pages = 1215&ndash;22  | pmid = 1846859 | issue = 3 | pmc = 207245 }}
 
{{hydrolase-stub}}
 
[[Category:EC 3.5.2]]
[[Category:Enzymes of unknown structure]]

Latest revision as of 09:20, 16 December 2014

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