Lipoat—protein ligaza
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| Lipoat—protein ligaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.7.63 | ||||||||
| CAS broj | 144114-18-1 | ||||||||
| 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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Lipoat—protein ligaza (EC 2.7.7.63, LplA, lipoat proteinska ligaza, lipoat-proteinska ligaza A, LPL, LPL-B) je enzim sa sistematskim imenom ATP:lipoat adenililtransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
Za rad ovog enzima je neophodan jon Mg2+.
Reference[uredi | uredi kod]
- ↑ Morris, T.W., Reed, K.E. and Cronan, J.E., Jr. (1994). „Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product”. J. Biol. Chem. 269: 16091-16100. PMID 8206909.
- ↑ Green, D.E., Morris, T.W., Green, J., Cronan, J.E., Jr. and Guest, J.R. (1995). „Purification and properties of the lipoate protein ligase of Escherichia coli”. Biochem. J. 309: 853-862. PMID 7639702.
- ↑ 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.
- ↑ Kim do, J., Kim, K.H., Lee, H.H., Lee, S.J., Ha, J.Y., Yoon, H.J. and Suh, S.W. (2005). „Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains”. J. Biol. Chem. 280: 38081-38089. PMID 16141198.
- ↑ Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A. and Taniguchi, H. (2005). „Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site”. J. Biol. Chem. 280: 33645-33651. PMID 16043486.
- ↑ 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.
- ↑ 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.
Literatura[uredi | uredi kod]
- 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.