View source for Biology:N-carbamoyl-D-amino acid hydrolase

{{infobox enzyme
| Name       = N-carbamoyl-D-amino acid hydrolase
| EC_number  = 3.5.1.77
| CAS_number = 71768-08-6
| GO_code    = 0047417
| image      =
| width      = 
| caption    =  
}}
In [[Biology:Enzymology|enzymology]], a '''N-carbamoyl-D-amino acid hydrolase''' ({{EC number|3.5.1.77}}) is an [[Biology:Enzyme|enzyme]] that [[Chemistry:Catalysis|catalyzes]] the [[Chemistry:Chemical reaction|chemical reaction]]

:N-carbamoyl-D-amino acid + H<sub>2</sub>O <math>\rightleftharpoons</math> D-amino acid + NH<sub>3</sub> + CO<sub>2</sub>

Thus, the two [[Biology:Substrate (biochemistry)|substrates]] of this enzyme are N-carbamoyl-D-amino acid and [[Chemistry:Water|H<sub>2</sub>O]], whereas its 3 [[Chemistry:Product|products]] are D-amino acid, [[Chemistry:Ammonia|NH<sub>3</sub>]], and [[Chemistry:Carbon dioxide|CO<sub>2</sub>]].

This enzyme belongs to the family of [[Biology:Hydrolase|hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides.

==Structural studies==

As of late 2007, 7 [[Biology:Tertiary structure|structures]] have been solved for this class of enzymes, with [[Biology:Protein Data Bank|PDB]] accession codes {{PDB link|1ERZ}}, {{PDB link|1UF4}}, {{PDB link|1UF5}}, {{PDB link|1UF7}}, {{PDB link|1UF8}}, {{PDB link|2GGK}}, and {{PDB link|2GGL}}.

==References==
{{reflist|1}}
* {{cite journal | vauthors = Ogawa J, Shimizu S, Yamada H | date = 1993 | title = N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization | journal = Eur. J. Biochem.  | volume = 212 | pages = 685&ndash;91  | pmid = 8462543 | doi = 10.1111/j.1432-1033.1993.tb17706.x | issue = 3 | doi-access = free }}

{{Carbon-nitrogen non-peptide hydrolases}}
{{Enzymes}}

[[Category:EC 3.5.1]]
[[Category:Enzymes of known structure]]



{{Sourceattribution|N-carbamoyl-D-amino acid hydrolase}}