Glycerol phosphoric acid shuttle

Glycerol phosphoric acid shuttle

A glycerol phosphoric acid shuttle (Glycerol phosphate shuttle) or the glycerol-3-phosphate Le Shuttle (Glycerol-3-phosphate shuttle) is one of the mechanism to regenerate NAD+ from the NADH which occurred as a by-product in cytoplasmic glycolytic pathway in a eukaryote. There is it to an animal [¹], a fungal [²] plant [³], protist [⁴] widely.

Table of contents

Background

NAD+/NADH becomes the coenzyme of the oxidation-reduction enzyme in the intracellular various metabolism system and has work to carry an electron from a certain reaction to other reactions. Because it is an oxidation reaction, and oxidized NAD+ thereby changes into reduced NADH if the catabolism is the large frame and sees it, it is necessary to oxidize NADH again to continue metabolism. When there is a eukaryote in an aerobic condition, a mitochondrial electronic transmission system generally oxidizes NADH using molecularity oxygen and I use a reduction power effectively and compose ATP. However, structure to oxidize the NADH which occurred with cytoplasm again efficiently is necessary because the NADH cannot penetrate mitochondrial lining membrane.

The glycerol phosphoric acid shuttle is one of such structure, and, besides, various mechanism is known. Malate - aspartic acid shuttle usually functions in mammals mainly, and the glycerol phosphoric acid shuttle functions only with a specific cell. Malate - oxaloacetic acid shuttle is known for the plant as well as malate - aspartic acid shuttle. In addition, there is type 2 NADH dehydrogenase oxidizing NADH on the cytoplasm side for a direct respiratory chain to a fungus or a plant. On the condition not to be able to perform oxygen breathing, I reproduce, for example, NAD+ by lactic fermentation.

Mechanism

The glycerol phosphoric acid shuttle is comprised of FAD dependence glycerol-3-phosphate dehydrogenase (mGPDH; EC 1.1.5.3) which is superficial on NAD-dependent glycerol-3-phosphate dehydrogenase (cGPDH; EC 1.1.1.8) in the cytoplasm and the mitochondrial intimal intermembrane space side.

Cytoplasmic cGPDH oxidizes NADH in NAD+ and returns dihydroxyacetone phosphoric acid (DHAP) to glycerol 3 - phosphoric acid (G3P). Molecular weight is small, and G3P and DHAP can pass mitochondrial adventitia freely through ポリン. In that way G3P which was in the intermembrane space is oxidized in DHAP by mGPDH on the mitochondrial lining membrane, and DHAP which occurred comes back to the cytoplasm. Because mGPDH returns ubiquinone (CoQ10) of the electronic transmission system through FAD of the coenzyme then, I form proton concentration gradient by work of complex III and complex IV and can make use for oxidative phosphorylation.

History

Pennsylvania University Bertram Sacktor and others proposed [⁷], that a shuttle system consisting of two glycerol-3-phosphate dehydrogenase existed in a flight line independently each using a housefly [⁵] [⁶] using a migratory locust Ernst Zebe and others of the Marburg University again from 1956 through 1959. It was revealed that there was it to the brown adipose tissue of the hamster when it was 1975, and it came to be thought that I had physiological importance in the mammals [⁸].

Allied item

• Mitochondrial shuttle system

References

1. ^ Mráček T, et al. (2013). "The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues." Biochim. Biophys. Acta 1827 (3): 401-410. doi: 10.1016/j.bbabio.2012.11.014. 
2. ^ Rigoulet M, et al. (2004). "Organization and regulation of the cytosolic NADH metabolism in the yeast Saccharomyces cerevisiae." Mol. Cell. Biochem. 256-257 (1-2): 73-81. PMID 14977171. 
3. ^ Shen W, et al. (2006). "Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NA^D+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis". Plant Cell 18 (2): 422–441. doi: 10.1105/tpc.105.039750. It is http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356549. PMC 1356549 
4. ^ Guerra DG, et al. (2006). "The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase of Trypanosomatidae and the glycosomal redox balance of insect stages of Trypanosoma brucei and Leishmania spp.." Mol. Biochem. Parasitol. 149 (2): 155-169. doi: 10.1016/j.molbiopara.2006.05.006. 
5. ^ H. Zebe, A. Delbrück, T. Bücher (1957). "Glycerophosphatdehydrogenase unter zellphysiologischen Aspekten." Ber. ges. Physiol. exp. Pharmakol.. 189. Tagung der Deutschen Gesellschaft für Physiol. Chemie, Hamburg, Sept. 1956. pp. 115-116 
6. ^ E. Zebe, A. Delbrück, Th. Bücher (1959). "Über den Glycerin-1-P-Cyclus im Flugmuskel von Locusta migratoria." Biochem. Z. It is 254-272 331. 
7. ^ Estabrook RW & Sacktor B (1958). "α-Glycerophosphate oxidase of flight muscle mitochondria." J. Biol. Chem. 233 (4): 1014-1019. 
8. ^ Houstĕk J, et al. (1975). "Gylcerol-3-phosphate shuttle and its function in intermediary metabolism of hamster brown-adipose tissue." Eur. J. Biochem. 54 (1): 11-18. doi: 10.1111/j.1432-1033.1975.tb04107.x. 

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