Lipoil (oktanoil) transferaza
| Lipoil (oktanoil) transferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.181 | ||||||||
| CAS broj | 392687-64-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Lipoil (oktanoil) transferaza (EC 2.3.1.181, LipB, lipoil (oktanoil)-(acil-nosilac-protein)-protein N-lipoiltransferaza, lipoil (oktanoil)-acil nosilac protein:protein transferaza, lipoat/oktanoatna transferaza, lipoiltransferaza, oktanoil-(acil nosilac protein)-protein N-oktanoiltransferaza, oktanoil-(acil-nosilac-protein):protein N-oktanoiltransferaza) je enzim sa sistematskim imenom oktanoil-(acil-nosilac protein):protein N-oktanoiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- oktanoil-[acil-nosilac protein] + protein protein N6-(oktanoil)lizin + [acil-nosilac protein]
Ovaj enzim posreduje prvi korak biosinteze lipoilnog kofaktora.
- ↑ 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.
- ↑ Vanden Boom, T.J., Reed, K.E. and Cronan, J.E., Jr. (1991). „Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system”. J. Bacteriol. 173: 6411-6420. PMID 1655709.
- ↑ Jordan, S.W. and Cronan, J.E., Jr. (1997). „A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria”. J. Biol. Chem. 272: 17903-17906. PMID 9218413.
- ↑ Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E. (2003). „Assembly of the covalent linkage between lipoic acid and its cognate enzymes”. Chem. Biol. 10: 1293-1302. PMID 14700636.
- ↑ Wada, M., Yasuno, R., Jordan, S.W., Cronan, J.E., Jr. and Wada, H. (2001). „Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase”. Plant Cell Physiol. 42: 650-656. PMID 11427685.
- ↑ 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.
- 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.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.