L-ribuloza-5-fosfatna 4-epimeraza
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| L-ribuloza-5-fosfatna 4-epimeraza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 5.1.3.4 | ||||||||
| CAS broj | 9024-19-5 | ||||||||
| 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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L-ribuloza-5-fosfatna 4-epimeraza (EC 5.1.3.4, fosforibulozna izomeraza, ribuloza fosfat 4-epimeraza, L-ribuloza-fosfat 4-epimeraza, L-ribuloza 5-fosfatna 4-epimeraza, AraD, L-Ru5P) je enzim sa sistematskim imenom L-ribuloza-5-fosfat 4-epimeraza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-ribuloza 5-fosfat D-ksiluloza 5-fosfat
Za dejstvo ovog enzima je neophodan divalentni katjon.
Reference[uredi - уреди | uredi kôd]
- ↑ Burma, D.P. and Horecker, B.L. (1958). „IV. <stereo>L</stereo>-Ribulose-5-phosphate 4-epimerase. Pentose formation by Lactobacillus plantarum”. J. Biol. Chem. 231: 1053-1064. PMID 13539036.
- ↑ Deupree, J.D. and Wood, W.A. (1970). „L-Ribulose 5-phosphate 4-epimerase of Aerobacter aerogenes. Evidence for nicotinamide adenine dinucleotide-independent 4-epimerization by the crystalline enzyme”. J. Biol. Chem. 245: 3988-3995. PMID 4395381.
- ↑ Lee, N., Patrick, J.W. and Masson, M. (1968). „Crystalline L-ribulose 5-phosphate 4-epimerase from Escherichia coli”. J. Biol. Chem. 243: 4700-4705. PMID 4879898.
- ↑ Wolin, M.J., Simpson, F.J. and Wood, W.A. (1958). „Degradation of L-arabinose by Aerobacter aerogenes. III. Identification and properties of L-ribulose-5-phosphate 4-epimerase”. J. Biol. Chem. 232: 559-575. PMID 13549442.
- ↑ Andersson, A., Schneider, G. and Lindqvist, Y. (1995). „Purification and preliminary X-ray crystallographic studies of recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia coli”. Protein Sci. 4: 1648-1650. PMID 8520491.
- ↑ Lee, L.V., Poyner, R.R., Vu, M.V. and Cleland, W.W. (2000). „Role of metal ions in the reaction catalyzed by L-ribulose-5-phosphate 4-epimerase”. Biochemistry 39: 4821-4830. PMID 10769139.
- ↑ Samuel, J., Luo, Y., Morgan, P.M., Strynadka, N.C. and Tanner, M.E. (2001). „Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase”. Biochemistry 40: 14772-14780. PMID 11732896.
Literatura[uredi - уреди | uredi kôd]
- 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. http://books.google.com/books/about/Fundamentals_of_enzymology.html?id=8uvwAAAAMAAJ.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. http://books.google.com/books/about/Advances_in_Enzymology_and_Related_Areas.html?id=Pmh8yToeuloC.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. http://www.garlandscience.com/textbooks/0815323042.asp?type=reviews.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. http://books.google.com/books/about/Enzyme_Kinetics.html?id=T60oAAAAYAAJ.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. http://books.google.com/books/about/Evaluation_of_Enzyme_Inhibitors_in_Drug.html?id=l2rMy8QNUk0C.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. http://books.google.com/books/about/Biochemical_pathways.html?id=081qAAAAMAAJ.
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