View source for Glycerol-3-phosphate dehydrogenase (quinone)

{{Infobox enzyme
| Name       = Glycerol-3-phosphate dehydrogenase
| EC_number  = 1.1.5.3
| CAS_number = 9001-49-4
| GO_code    =
| image      = 2r46.jpg
| width      = 270
| caption    = Glycerol-3-phosphate dehydrogenase monomer + FAD, E.Coli
| AltNames   = valpha-glycerophosphate dehydrogenase, alpha-glycerophosphate dehydrogenase (acceptor), anaerobic glycerol-3-phosphate dehydrogenase, DL-glycerol 3-phosphate oxidase (misleading), FAD-dependent glycerol-3-phosphate dehydrogenase, FAD-dependent sn-glycerol-3-phosphate dehydrogenase, FAD-GPDH, FAD-linked glycerol 3-phosphate dehydrogenase, FAD-linked L-glycerol-3-phosphate dehydrogenase, flavin-linked glycerol-3-phosphate dehydrogenase, flavoprotein-linked L-glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate cytochrome c reductase (misleading), glycerol phosphate dehydrogenase, glycerol phosphate dehydrogenase (acceptor), glycerol phosphate dehydrogenase (FAD), glycerol-3-phosphate CoQ reductase, glycerol-3-phosphate dehydrogenase (flavin-linked), glycerol-3-phosphate:CoQ reductase, glycerophosphate dehydrogenase, L-3-glycerophosphate-ubiquinone oxidoreductase, L-glycerol-3-phosphate dehydrogenase (ambiguous), L-glycerophosphate dehydrogenase, mGPD, mitochondrial glycerol phosphate dehydrogenase, NAD+-independent glycerol phosphate dehydrogenase, pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase, sn-glycerol 3-phosphate oxidase (misleading), sn-glycerol-3-phosphate dehydrogenase, sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase, sn-glycerol-3-phosphate:acceptor 2-oxidoreductase) 
}}
'''Glycerol-3-phosphate dehydrogenase''' ({{EC number|1.1.5.3}} is an [[enzyme]] with [[List of enzymes|systematic name]] sn-glycerol 3-phosphate:quinone oxidoreductase.<ref>{{cite journal | vauthors = Ringler RL | title = Studies on the mitochondrial alpha-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain | journal = The Journal of Biological Chemistry | volume = 236 | pages = 1192–8 | date = April 1961 | issue = 4 | doi = 10.1016/S0021-9258(18)64266-8 | doi-access = free | pmid = 13741763 }}</ref><ref>{{cite journal | vauthors = Schryvers A, Lohmeier E, Weiner JH | title = Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli | journal = The Journal of Biological Chemistry | volume = 253 | issue = 3 | pages = 783–8 | date = February 1978 | doi = 10.1016/S0021-9258(17)38171-1 | doi-access = free | pmid = 340460 }}</ref><ref>{{cite journal | vauthors = MacDonald MJ, Brown LJ | title = Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied | journal = Archives of Biochemistry and Biophysics | volume = 326 | issue = 1 | pages = 79–84 | date = February 1996 | pmid = 8579375 | doi = 10.1006/abbi.1996.0049 }}</ref><ref>{{cite journal | vauthors = Rauchová H, Fato R, Drahota Z, Lenaz G | title = Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria | journal = Archives of Biochemistry and Biophysics | volume = 344 | issue = 1 | pages = 235–41 | date = August 1997 | pmid = 9244403 | doi = 10.1006/abbi.1997.0150 }}</ref><ref>{{cite journal | vauthors = Shen W, Wei Y, Dauk M, Zheng Z, Zou J | title = Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants | journal = FEBS Letters | volume = 536 | issue = 1–3 | pages = 92–6 | date = February 2003 | pmid = 12586344 | doi = 10.1016/s0014-5793(03)00033-4 | doi-access = free | bibcode = 2003FEBSL.536...92S }}</ref><ref>{{cite journal | vauthors = Walz AC, Demel RA, de Kruijff B, Mutzel R | title = Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix | journal = The Biochemical Journal | volume = 365 | issue = Pt 2 | pages = 471–9 | date = July 2002 | pmid = 11955283 | pmc = 1222694 | doi = 10.1042/BJ20011853 }}</ref><ref>{{cite journal | vauthors = Ansell R, Granath K, Hohmann S, Thevelein JM, Adler L | title = The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation | journal = The EMBO Journal | volume = 16 | issue = 9 | pages = 2179–87 | date = May 1997 | pmid = 9171333 | pmc = 1169820 | doi = 10.1093/emboj/16.9.2179 }}</ref><ref>{{cite journal | vauthors = Larsson C, Påhlman IL, Ansell R, Rigoulet M, Adler L, Gustafsson L | title = The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae | journal = Yeast | volume = 14 | issue = 4 | pages = 347–57 | date = March 1998 | pmid = 9559543 | doi = 10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.0.CO;2-9 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: sn-glycerol 3-phosphate + quinone <math>\rightleftharpoons</math> glycerone phosphate + quinol

This flavin-dependent dehydrogenase is a membrane enzyme. It participates in glycolysis, respiration and phospholipid biosynthesis.

== References ==
{{reflist}}

== External links ==
* {{MeshName|Glycerol-3-phosphate+dehydrogenase}}

{{Alcohol oxidoreductases}}
{{Enzymes}}
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[[Category:EC 1.1.5]]