Piruvat dehidrogenaza (hinon)
| Piruvat dehidrogenaza (hinon) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.5.1 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Piruvat dehidrogenaza (hinon) (EC 1.2.5.1, piruvatna dehidrogenaza, piruvinska dehidrogenaza, piruvincka (citohrom b1) dehidrogenaza, piruvat:ubihinon-8-oksidoreduktaza, piruvatna oksidaza (nespecifična), piruvatna dehidrogenaza (citohrom)) je enzim sa sistematskim imenom piruvat:ubihinon oksidoreduktaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
Ovaj enzim je flavoprotein (FAD). On je bakterijski enzim lociran na unutrašnjoj površini citoplazmične membrane i spregnut je sa respiratorim lancem putem ubihinona. On ne deluje na menahinon. Njegu aktivnost znatno povećavaju lipidi. Za njegov rad je neophodan tiamin difosfat. Ovaj enzim takođe može da formira acetoin.
Reference[уреди | уреди извор]
- ^ Recny, M.A. & Hager, L.P. (1982). „Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD”. J. Biol. Chem. 257: 12878—12886. PMID 6752142.
- ^ Cunningham, C.C. & Hager, L.P. (1975). „Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids”. J. Biol. Chem. 250: 7139—7146. PMID 1100621.
- ^ Koland, J.G., Miller, M.J. and Gennis, R.B. (1984). „Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase”. Biochemistry. 23: 445—453. PMID 6367818.
- ^ Grabau, C. & Cronan, J.E., Jr. (1986). „In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site”. Biochemistry. 25: 3748—3751. PMID 3527254.
- ^ Wang, A.Y., Chang, Y.Y. and Cronan, J.E., Jr. (1991). „Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding”. J. Biol. Chem. 266: 10959—10966. PMID 2040613.
- ^ Chang, Y.Y. & Cronan, J.E., Jr. (1997). „Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase”. Biochemistry. 36: 11564—11573. PMID 9305946.
- ^ O'Brien, T.A., Schrock, H.L., Russell, P., Blake, R., 2nd and Gennis, R.B. (1976). „Preparation of Escherichia coli pyruvate oxidase utilizing a thiamine pyrophosphate affinity column”. Biochim. Biophys. Acta. 452: 13—29. PMID 791368.
- ^ Bertagnolli, B.L. & Hager, L.P. (1993). „Role of flavin in acetoin production by two bacterial pyruvate oxidases”. Arch. Biochem. Biophys. 300: 364—371. PMID 8424670.
Literatura[уреди | уреди извор]
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze[уреди | уреди извор]
- Pyruvate+dehydrogenase+(quinone) на US National Library of Medicine Medical Subject Headings (MeSH)
