N-acetyl-gamma-glutamyl-phosphate reductase: Difference between revisions

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{{enzyme
| Name = pyruvate oxidase
| EC_number = 1.2.3.3
| CAS_number = 9001-96-1
| IUBMB_EC_number = 1/2/3/3
| GO_code = 0047112
| image =
| width =
| caption =
}}
In [[enzymology]], a '''pyruvate oxidase''' ({{EC number|1.2.3.3}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]


:pyruvate + phosphate + O<sub>2</sub> <math>\rightleftharpoons</math> acetyl phosphate + CO<sub>2</sub> + H<sub>2</sub>O<sub>2</sub>


The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[pyruvate]], [[phosphate]], and [[oxygen|O<sub>2</sub>]], whereas its 3 [[product (chemistry)|products]] are [[acetyl phosphate]], [[carbon dioxide|CO<sub>2</sub>]], and [[hydrogen peroxide|H<sub>2</sub>O<sub>2</sub>]].
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This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is '''pyruvate:oxygen 2-oxidoreductase (phosphorylating)'''. Other names in common use include '''pyruvic oxidase''', and '''phosphate-dependent pyruvate oxidase'''. This enzyme participates in [[pyruvate metabolism]]. It has 2 [[cofactor (biochemistry)|cofactors]]: [[FAD]],  and [[Thiamin diphosphate]].
 
==Structural studies==
 
As of late 2007, 12 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1POW}}, {{PDB link|1POX}}, {{PDB link|1V5E}}, {{PDB link|1V5F}}, {{PDB link|1V5G}}, {{PDB link|1Y9D}}, {{PDB link|2DJI}}, {{PDB link|2EZ4}}, {{PDB link|2EZ8}}, {{PDB link|2EZ9}}, {{PDB link|2EZT}}, and {{PDB link|2EZU}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = Williams FR, Hager LP | date = 1966 | title = Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein | journal = Arch. Biochem. Biophys. | volume = 116 | pages = 168&ndash;76  | pmid = 5336022 | doi = 10.1016/0003-9861(66)90025-7 | issue = 1 }}
* {{cite journal | author = Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G | date = 2005 | title = Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair | journal = Biochemistry.  | volume = 44 | pages = 13291&ndash;303  | pmid = 16201755 | doi = 10.1021/bi051058z | issue = 40 }}
 
{{1.2-enzyme-stub}}
 
[[Category:EC 1.2.3]]
[[Category:Flavin enzymes]]
[[Category:Thiamin diphosphate enzymes]]
[[Category:Enzymes of known structure]]

Latest revision as of 14:48, 26 May 2014


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