Inozitol-polifosfatna 5-fosfataza
| Inozitol-polifosfatna 5-fosfataza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.3.56 | ||||||||
| CAS broj | 106283-14-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Inozitol-polifosfatna 5-fosfataza (EC 3.1.3.56, tip I inozitol-polifosfatna fosfataza, inozitol trisfosfatna fosfomonoesteraza, InsP3/Ins(1,3,4,5)P4 5-fosfataza, inozinska trifosfataza, D-mio-inozitol 1,4,5-trifosfat 5-fosfataza, D-mio-inozitol 1,4,5-trisfosfat 5-fosfataza, L-mio-inozitol 1,4,5-trisfosfat-monoesteraza, inozitol fosfat 5-fosfomonoesteraza, inozitol-1,4,5-trisfosfat/1,3,4,5-tetrakisfosfat 5-fosfataza, Ins(1,4,5)P3 5-fosfataza, D-mio-inozitol(1,4,5)/(1,3,4,5)-polifosfat 5-fosfataza, inozitol 1,4,5-trisfosfat fosfataza, inozitol polifosfat-5-fosfataza, mio-inozitol-1,4,5-trisfosfat 5-fosfataza, inozitol-1,4,5-trisfosfat 5-fosfataza) je enzim sa sistematskim imenom 1D-mio-inozitol-1,4,5-trisfosfat 5-fosfohidrolaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) D-mio-inozitol 1,4,5-trisfosfat + H2O mio-inozitol 1,4-bisfosfat + fosfat
- (2) 1D-mio-inozitol 1,3,4,5-tetrakisfosfat + H2O 1D-mio-inozitol 1,3,4-trisfosfat + fosfat
Jedna sisarska izoforma je poznata.
Reference[uredi | uredi kod]
- ↑ Downes, C.P., Mussat, M.C. and Michell, R.H. (1982). „The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane”. Biochem. J. 203: 169-177. PMID 6285891.
- ↑ Erneux, C., Lemos, M., Verjans, B., Vanderhaeghen, P., Delvaux, A. and Dumont, J.E. (1989). „Soluble and particulate Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase in bovine brain”. Eur. J. Biochem. 181: 317-322. PMID 2540972.
- ↑ Woscholski, R. and Parker, P.J. (2000). „Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates”. u: Cockcroft, S.. Biology of Phosphoinositides. Oxford: Biology of Phosphoinositides. str. 320-338.
- ↑ Verjans, B., De Smedt, F., Lecocq, R., Vanweyenberg, V., Moreau, C. and Erneux, C. (1994). „Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase”. Biochem. J. 300: 85-90. PMID 8198557.
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.
- Woscholski, R. and Parker, P.J. (2000). „Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates”. u: Cockcroft, S.. Biology of Phosphoinositides. Oxford: Biology of Phosphoinositides. str. 320-338.