Glycerol-3-phosphate dehydrogenase (quinone)

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Glycerol-3-phosphate dehydrogenase
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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.

Related Research Articles

<span class="mw-page-title-main">Glycolysis</span> Catabolic pathway

Glycolysis is the metabolic pathway that converts glucose into pyruvate, and in most organisms, occurs in the liquid part of cells, the cytosol. The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes.

<span class="mw-page-title-main">Oxidative phosphorylation</span> Metabolic pathway

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

<span class="mw-page-title-main">Electron transport chain</span> Energy-producing metabolic pathway

An electron transport chain (ETC) is a series of protein complexes and other molecules that transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. The electrons that are transferred from NADH and FADH2 to the ETC involves four multi-subunit large enzymes complexes and two mobile electron carriers. Many of the enzymes in the electron transport chain are embedded within the membrane.

<span class="mw-page-title-main">Cellular respiration</span> Process to convert glucose to ATP in cells

Cellular respiration is the process by which biological fuels are oxidised in the presence of an inorganic electron acceptor, such as oxygen, to drive the bulk production of adenosine triphosphate (ATP), which contains energy. Cellular respiration may be described as a set of metabolic reactions and processes that take place in the cells of organisms to convert chemical energy from nutrients into ATP, and then release waste products.

<span class="mw-page-title-main">Succinate dehydrogenase</span> Enzyme

Succinate dehydrogenase (SDH) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex, found in many bacterial cells and in the inner mitochondrial membrane of eukaryotes. It is the only enzyme that participates in both the citric acid cycle and the electron transport chain. Histochemical analysis showing high succinate dehydrogenase in muscle demonstrates high mitochondrial content and high oxidative potential.

<span class="mw-page-title-main">Malate-aspartate shuttle</span> Biochemical system for transporting electrons produced during glycolysis

The malate-aspartate shuttle is a biochemical system for translocating electrons produced during glycolysis across the semipermeable inner membrane of the mitochondrion for oxidative phosphorylation in eukaryotes. These electrons enter the electron transport chain of the mitochondria via reduction equivalents to generate ATP. The shuttle system is required because the mitochondrial inner membrane is impermeable to NADH, the primary reducing equivalent of the electron transport chain. To circumvent this, malate carries the reducing equivalents across the membrane.

sn-Glycerol 3-phosphate is the organic ion with the formula HOCH2CH(OH)CH2OPO32-. It is one of three stereoisomers of the ester of dibasic phosphoric acid (HOPO32-) and glycerol. It is a component of glycerophospholipids. From a historical reason, it is also known as L-glycerol 3-phosphate, D-glycerol 1-phosphate, L-α-glycerophosphoric acid.

<span class="mw-page-title-main">Glycerol kinase</span> Enzyme

Glycerol kinase, encoded by the gene GK, is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis.

<span class="mw-page-title-main">Glycerol phosphate shuttle</span>

The glycerol-3-phosphate shuttle is a mechanism used in skeletal muscle and the brain that regenerates NAD+ from NADH, a by-product of glycolysis. The NADH generated during glycolysis is found in the cytoplasm and must be transported into the mitochondria to enter the oxidative phosphorylation pathway. However, the inner mitochondrial membrane is impermeable to NADH and NAD+ and does not contain a transport system for these electron carriers. Either the glycerol-3-phosphate shuttle pathway or the malate-aspartate shuttle pathway, depending on the tissue of the organism, must be taken to transport cytoplasmic NADH into the mitochondria. The shuttle consists of the sequential activity of two proteins; Cytoplasmic glycerol-3-phosphate dehydrogenase (cGPD) transfers an electron pair from NADH to dihydroxyacetone phosphate (DHAP), forming glycerol-3-phosphate (G3P) and regenerating NAD+ needed to generate energy via glycolysis. The other protein, mitochondrial glycerol-3-phosphate dehydrogenase (mGPD) catalyzes the oxidation of G3P by FAD, regenerating DHAP in the cytosol and forming FADH2 in the mitochondrial matrix. In mammals, its activity in transporting reducing equivalents across the mitochondrial membrane is considered secondary to the malate-aspartate shuttle.

<span class="mw-page-title-main">2,4 Dienoyl-CoA reductase</span> Class of enzymes

2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes the following reactions

<span class="mw-page-title-main">Glycerol-3-phosphate dehydrogenase</span> Class of enzymes

Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate to sn-glycerol 3-phosphate.

In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) is an enzyme that catalyzes the chemical reaction

In enzymology, a quinoprotein glucose dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NAD(P)H dehydrogenase (quinone)</span>

In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a glycerol-3-phosphate O-acyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Dihydroorotate dehydrogenase (quinone)</span> Class of enzymes

Class 2 dihydroorotate dehydrogenases is an enzyme with systematic name (S)-dihydroorotate:quinone oxidoreductase. This enzyme catalyses the electron transfer from dihydroorotate to a quinone :

<span class="mw-page-title-main">Fumarate reductase (quinol)</span>

Fumarate reductase (quinol) (EC 1.3.5.4, QFR,FRD, menaquinol-fumarate oxidoreductase, quinol:fumarate reductase) is an enzyme with systematic name succinate:quinone oxidoreductase. This enzyme catalyzes the following chemical reaction:

Pyruvate dehydrogenase (quinone) (EC 1.2.5.1, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction

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.