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Ascaris suum pyruvate dehydrogenase complex

Metabolic Transitions and the Role of the Pyruvate Dehydrogenase Complex During Development of Ascaris suum... [Pg.277]

Fig. 14.1. Role ofthe pyruvate dehydrogenase complex (PDC) during aerobic/ anaerobic transitions in the development of Ascaris suum. PDC, pyruvate dehydrogenase complex AD, acyl CoA dehydrogenase ER, enoyl CoA reductase FR, fumarate reductase SDH, succinate dehydrogenase. Fig. 14.1. Role ofthe pyruvate dehydrogenase complex (PDC) during aerobic/ anaerobic transitions in the development of Ascaris suum. PDC, pyruvate dehydrogenase complex AD, acyl CoA dehydrogenase ER, enoyl CoA reductase FR, fumarate reductase SDH, succinate dehydrogenase.
Klingbeil, M.M., Walker, D.J., Arnette, R., Sidawy, E., Hayton, K, Komuniecki, P.R. and Komuniecki, R. (1996) Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum. Journal of Biological Chemistry 271, 5451-5457. [Pg.289]

Thissen, J., Desai, S., McCartney, P. and Komuniecki, R. (1986) Improved purification of the pyruvate dehydrogenase complex from Ascaris suum body wall muscle and characterization of PDHa kinase activity. Molecular and Biochemical Parasitology 21, 129-138. [Pg.291]

Komuniecki, R., Rhee, R., Bhat, D., Duran, E., Sidawy. E. and Song, H. (1992) The pyruvate dehydrogenase complex from the parasitic nematode, Ascaris suum novel subunit composition and domain structure of the dihydrolipoyl transacetylase component. Arch. Biochem. Biophys. 296 115 121. [Pg.65]

Komuniecki, R. and Thissen, J. (1989) The pyruvate dehydrogenase complex from the parasitic nematode, Ascaris suum stoichiometry of phosphorylation and inactivation. Ann. [Pg.65]

In the oxidative branch of malate dismutation, malic enzyme oxidizes malate to pyruvate, which is then further oxidized to acetyl-CoA by pyruvate dehydrogenase, an enzyme complex specially adapted to anaerobic functioning in Ascaris suum and possibly in other parasitic helminths like the trematode F. hepatica and the cestode Dipylidium caninum (Diaz and Komuniecki, 1994 Klingbeil et al., 1996). Parasitic helminths like F. hepatica use an acetate succinate CoA-transferase (ASCT) for... [Pg.391]

Fig. 5.2. Possible metabolic pathways in facultative anaerobic mitochondria. Shaded boxes show components of the electron-transport chain used during hypoxia, open boxes are components used during aerobiosis, and the hatched boxes (complex I and ATP-synthase) are components used under aerobic as well as anaerobic conditions. ASCT acetate succinate CoA-transferase, C cytochrome c, Cl, CIII and CIV complexes I, III and IV of the respiratory chain, CITR citrate, ECR enoyl-CoA reductase (such as present in Ascaris suum), ETF electron-transfer flavoprotein, ETF RQ OR electron-transfer flavoproteimrhodoquinone oxidoreductase, FRD fumarate reductase, FUM fumarate, MAE malate, OXAC oxaloacetate, PYR pyruvate, RQ rhodoquinone, SDH succinate dehydrogenase, SUCC succinate, Succ-CoA succinyl-CoA, TER trans-2-enoyl-CoA reductase (such as present in E. gracilis), UQ ubiquinone... Fig. 5.2. Possible metabolic pathways in facultative anaerobic mitochondria. Shaded boxes show components of the electron-transport chain used during hypoxia, open boxes are components used during aerobiosis, and the hatched boxes (complex I and ATP-synthase) are components used under aerobic as well as anaerobic conditions. ASCT acetate succinate CoA-transferase, C cytochrome c, Cl, CIII and CIV complexes I, III and IV of the respiratory chain, CITR citrate, ECR enoyl-CoA reductase (such as present in Ascaris suum), ETF electron-transfer flavoprotein, ETF RQ OR electron-transfer flavoproteimrhodoquinone oxidoreductase, FRD fumarate reductase, FUM fumarate, MAE malate, OXAC oxaloacetate, PYR pyruvate, RQ rhodoquinone, SDH succinate dehydrogenase, SUCC succinate, Succ-CoA succinyl-CoA, TER trans-2-enoyl-CoA reductase (such as present in E. gracilis), UQ ubiquinone...



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Ascaris suum

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Pyruvate dehydrogenase complex

Pyruvate dehydrogenases

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