View source for Long-chain acyl-CoA dehydrogenase

{{Infobox enzyme
| Name = Pyruvate dehydrogenase (quinone)
| EC_number = 1.2.5.1
| CAS_number = 
| IUBMB_EC_number = 1/2/5/1
| GO_code = 
| image = 
| width = 
| caption =
}}
'''Pyruvate dehydrogenase (quinone)''' ({{EC number|1.2.5.1}}, ''pyruvate dehydrogenase'', ''pyruvic dehydrogenase'', ''pyruvic (cytochrome b1) dehydrogenase'', ''pyruvate:ubiquinone-8-oxidoreductase'', ''pyruvate oxidase (ambiguous)'') is an [[enzyme]] with system name ''pyruvate:ubiquinone oxidoreductase''.<ref>{{cite journal | title = Reconstitution of native <em>Escherichia coli</em> pyruvate oxidase from apoenzyme monomers and FAD |author = Recny, M.A. and Hager, L.P. |journal = J. Biol. Chem. |date = 1982 |volume = 257 |pages = 12878–12886 |pmid = 6752142 | issue = 21}}</ref><ref>{{cite journal | title = Reactivation of the lipid-depleted pyruvate oxidase system from <em>Escherichia coli</em> with cell envelope neutral lipids |author = Cunningham, C.C. and Hager, L.P. |journal = J. Biol. Chem. |date = 1975 |volume = 250 |pages = 7139–7146 |pmid = 1100621 | issue = 18}}</ref><ref>{{cite journal | title = Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of <em>Escherichia coli</em> with the cytochrome <em>d</em>  terminal oxidase |author = Koland, J.G., Miller, M.J. and Gennis, R.B. |journal = Biochemistry |date = 1984 |volume = 23 |pages = 445–453 |pmid = 6367818 | doi = 10.1021/bi00298a008 | issue = 3}}</ref><ref>{{cite journal | title = <em>In vivo</em> function of <em>Escherichia coli</em> pyruvate oxidase specifically requires a functional lipid binding site |author = Grabau, C. and Cronan, J.E., Jr. |journal = Biochemistry |date = 1986 |volume = 25 |pages = 3748–3751 |pmid = 3527254 | doi = 10.1021/bi00361a003 | issue = 13}}</ref><ref>{{cite journal | title = Role of the tetrameric structure of <em>Escherichia coli</em> pyruvate oxidase in enzyme activation and lipid binding |author = Wang, A.Y., Chang, Y.Y. and Cronan, J.E., Jr. |journal = J. Biol. Chem. |date = 1991 |volume = 266 |pages = 10959–10966 |pmid = 2040613 | issue = 17}}</ref><ref>{{cite journal | title = Sulfhydryl chemistry detects three conformations of the lipid binding region of <em>Escherichia coli</em> pyruvate oxidase |author = Chang, Y.Y. and Cronan, J.E., Jr. |journal = Biochemistry |date = 1997 |volume = 36 |pages = 11564–11573 |pmid = 9305946 | doi = 10.1021/bi9709102 | issue = 39}}</ref><ref>{{cite journal | title = Preparation of <em>Escherichia coli</em> pyruvate oxidase utilizing a thiamine pyrophosphate affinity column |author = O'Brien, T.A., Schrock, H.L., Russell, P., Blake, R., 2nd and Gennis, R.B. |journal = Biochim. Biophys. Acta |date = 1976 |volume = 452 |pages = 13–29 |pmid = 791368 | issue = 1}}</ref><ref>{{cite journal | title = Role of flavin in acetoin production by two bacterial pyruvate oxidases |author = Bertagnolli, B.L. and Hager, L.P. |journal = Arch. Biochem. Biophys. |date = 1993 |volume = 300 |pages = 364–371 |pmid = 8424670 | doi = 10.1006/abbi.1993.1049 | issue = 1}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: [[pyruvate]] + [[ubiquinone]] + H<sub>2</sub>O <math>\rightleftharpoons</math> [[acetate]] + CO<sub>2</sub> + [[ubiquinol]]

This bacterial enzyme is located on the inner surface of the [[cytoplasmic membrane]].

== References ==
{{reflist}}

== External links ==
* {{MeshName|Pyruvate+dehydrogenase+(quinone)}}

[[Category:EC 1.2.5]]