Inozitol-3-fosfatna sintaza
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| Inozitol-3-fosfatna sintaza | |||||||||
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| Tetramer mio-inozitol-1-fosfat sintaze (srodan protein) (Thermotoga maritima) | |||||||||
| Identifikatori | |||||||||
| EC broj | 5.5.1.4 | ||||||||
| CAS broj | 9032-95-5 | ||||||||
| 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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Inozitol-3-fosfatna sintaza (EC 5.5.1.4, mio-inozitol-1-fosfat sintaza, D-glukoza 6-fosfat cikloaldolaza, inozitol 1-fosfatna sintataza, glukoza 6-fosfat ciklaza, inozitol 1-fosfatna sintetaza, glukoza-6-fosfat inozitol monofosfatna cikloaldolaza, glukocikloaldolaza, 1L-mio-inozitol-1-fosfat lijaza (izomerizacija)) je enzim sa sistematskim imenom 1D-mio-inozitol-3-fosfat lijaza (izomerizacija).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- D-glukoza 6-fosfat 1D-mio-inozitol 3-fosfat
Za dejstvo ovog enzima je neophodan NAD+.
Reference[uredi - уреди | uredi kôd]
- ↑ Eisenberg, F., Jr. (1967). „D-Myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis”. J. Biol. Chem. 242: 1375-1382. PMID 4290245.
- ↑ Sherman, W.R., Stewart, M.A. and Zinbo, M. (1969). „Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase”. J. Biol. Chem. 244: 5703-5708. PMID 4310603.
- ↑ Barnett, J.E.G. and Corina, D.L. (1968). „The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate cyclase of rat testis. The involvement of hydrogen atoms”. Biochem. J. 108: 125-129. PMID 4297937.
- ↑ Barnett, J.E.G., Rasheed, A. and Corina, D.L. (1973). „Partial reactions of glucose 6-phosphate-1L-myo-inositol 1-phosphate cyclase”. Biochem. J. 131: 21-30. PMID 4352864.
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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