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Glycerol-3-phosphate dehydrogenase (quinone)

From Wikipedia, the free encyclopedia

Glycerol-3-phosphate dehydrogenase
Glycerol-3-phosphate dehydrogenase monomer + FAD, E.Coli
Identifiers
EC no.1.1.5.3
CAS no.9001-49-4 
Alt. namesvalpha-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)
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Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3 is an enzyme with systematic name sn-glycerol 3-phosphate:quinone oxidoreductase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction

sn-glycerol 3-phosphate + quinone glycerone phosphate + quinol

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

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Transcription

References

  1. ^ Ringler RL (April 1961). "Studies on the mitochondrial alpha-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain". The Journal of Biological Chemistry. 236: 1192–8. PMID 13741763.
  2. ^ Schryvers A, Lohmeier E, Weiner JH (February 1978). "Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli". The Journal of Biological Chemistry. 253 (3): 783–8. PMID 340460.
  3. ^ MacDonald MJ, Brown LJ (February 1996). "Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied". Archives of Biochemistry and Biophysics. 326 (1): 79–84. doi:10.1006/abbi.1996.0049. PMID 8579375.
  4. ^ Rauchová H, Fato R, Drahota Z, Lenaz G (August 1997). "Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria". Archives of Biochemistry and Biophysics. 344 (1): 235–41. doi:10.1006/abbi.1997.0150. PMID 9244403.
  5. ^ Shen W, Wei Y, Dauk M, Zheng Z, Zou J (February 2003). "Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants". FEBS Letters. 536 (1–3): 92–6. doi:10.1016/s0014-5793(03)00033-4. PMID 12586344.
  6. ^ Walz AC, Demel RA, de Kruijff B, Mutzel R (July 2002). "Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix". The Biochemical Journal. 365 (Pt 2): 471–9. doi:10.1042/BJ20011853. PMC 1222694. PMID 11955283.
  7. ^ Ansell R, Granath K, Hohmann S, Thevelein JM, Adler L (May 1997). "The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation". The EMBO Journal. 16 (9): 2179–87. doi:10.1093/emboj/16.9.2179. PMC 1169820. PMID 9171333.
  8. ^ Larsson C, Påhlman IL, Ansell R, Rigoulet M, Adler L, Gustafsson L (March 1998). "The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae". Yeast. 14 (4): 347–57. doi:10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.0.CO;2-9. PMID 9559543.

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This page was last edited on 26 August 2023, at 14:20
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