Glycerol-3-phosphate dehydrogenase (quinone)

Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3, alpha-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) 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

\rightleftharpoons

glycerone phosphate + quinol

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

References

↑ Ringler, R.L. (1961). "Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain". J. Biol. Chem. 236: 1192–1198. PMID 13741763.
↑ Schryvers, A.; Lohmeier, E.; Weiner, J.H. (1978). "Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli". J. Biol. Chem. 253 (3): 783–788. PMID 340460.
↑ MacDonald, M.J.; Brown, L.J. (1996). "Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied". Arch. Biochem. Biophys. 326 (1): 79–84. doi:10.1006/abbi.1996.0049. PMID 8579375.
↑ Rauchová, H.; Fato, R.; Drahota, Z.; Lenaz, G. (1997). "Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria". Arch. Biochem. Biophys. 344 (1): 235–241. doi:10.1006/abbi.1997.0150. PMID 9244403.
↑ Shen, W.; Wei, Y.; Dauk, M.; Zheng, Z.; Zou, J. (2003). "Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants". FEBS Lett. 536 (1-3): 92–96. doi:10.1016/s0014-5793(03)00033-4. PMID 12586344.
↑ Walz, A.C.; Demel, R.A.; de Kruijff, B.; Mutzel, R. (2002). "Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix". Biochem. J. 365 (Pt 2): 471–479. doi:10.1042/BJ20011853. PMC 1222694. PMID 11955283.
↑ Ansell, R.; Granath, K.; Hohmann, S.; Thevelein, J.M.; Adler, L. (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". EMBO J. 16: 2179–2187. doi:10.1093/emboj/16.9.2179. PMC 1169820. PMID 9171333.
↑ Larsson, C.; Påhlman, I.L.; Ansell, R.; Rigoulet, M.; Adler, L.; Gustafsson, L. (1998). "The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae". Yeast. 14 (4): 347–357. doi:10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.0.CO;2-9. PMID 9559543.

External links

Glycerol-3-phosphate dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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