Dihidrolipoil dehidrogenaza
| Dihidrolipoil dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Dihidrolipoil dehidrogenaza dimer, Pseudomonas putida | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.8.1.4 | ||||||||
| CAS broj | 9001-18-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Dihidrolipoil dehidrogenaza (EC 1.8.1.4, LDP-Glc, LDP-Val, dehidrolipoatna dehidrogenaza, dijaforaza, dihidrolipoamidna dehidrogenaza, dihidrolipoamid:NAD+ oksidoreduktaza, dihidrolipoinska dehidrogenaza, dihidrotioktinska dehidrogenaza, lipoamidna dehidrogenaza (NADH), lipoamidna oksidoreduktaza (NADH), lipoamidna reduktaza, lipoamidna reduktaza (NADH), lipoatna dehidrogenaza, lipoinsko kiselinska dehidrogenaza, lipoilna dehidrogenaza, protein-6-N-(dihidrolipoil)lizin:NAD+ oksidoreduktaza) je enzim sa sistematskim imenom protein-N6-(dihidrolipoil)lizin:NAD+ oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- protein N6-(dihidrolipoil)lizin + NAD+ protein N6-(lipoil)lizin + NADH + H+
Ovaj enzim je flavoprotein (FAD). On je komponenta multienzimskog kompleksa 2-okso-kiselinske dehidrogenaze.
- ↑ Massey, V. (1963). „Lipoyl dehydrogenase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 275-306.
- ↑ Massey, V., Gibson, Q.H. and Veeger, C. (1960). „Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)”. Biochem. J. 77: 341-351. PMID 13767908.
- ↑ Savage, N. (1957). „Preparation and properties of highly purified diaphorase”. Biochem. J. 67: 146-155. PMID 13471525.
- ↑ Straub, F.B. (1939). „Isolation and properties of a flavoprotein from heart muscle tissue”. Biochem. J. 33: 787-792. PMID 16746974.
- ↑ Perham, R.N. (2000). „Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions”. Annu. Rev. Biochem. 69: 961-1004. PMID 10966480.
- ↑ Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. (2005). „Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase”. Protein Expr. Purif. 39: 269-282. PMID 15642479.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
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