Inozitol-fosfat fosfataza
| Inozitol-fosfat fosfataza | |||||||||
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| Inozitol-fosfat fosfataza dimer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.1.3.25 | ||||||||
| CAS broj | 37184-63-7 | ||||||||
| 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-fosfat fosfataza (EC 3.1.3.25, mio-inozitol-1(ili 4)-monofosfataza, inozitol 1-fosfataza, L-mio-inozitol-1-fosfat fosfataza, mio-inozitol 1-fosfataza, inozitolna fosfataza, inozitol monofosfatna fosfataza, inozitol-1(ili 4)-monofosfataza, mio-inozitol-1(ili 4)-fosfatna fosfohidrolaza, mio-inozitolna monofosfataza, mio-inozitol-1-fosfataza) je enzim sa sistematskim imenom mio-inozitol-fosfat fosfohidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- mio-inozitol fosfat + H2O mio-inozitol + fosfat
Ovaj enzim deluje na pet od šest mogućih izomera mio-inozitol fosfata, na sve sem mio-inozitol 2-fosfata.
Reference
- ↑ 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.
- ↑ Gee, N.S., Ragan, C.I., Watling, K.J., Aspley, S., Jackson, R.G., Reid, G.G., Gani, D. and Shute, J.K. (1988). „The purification and properties of myo-inositol monophosphatase from bovine brain”. Biochem. J. 249: 883-889. PMID 2833231.
- ↑ Hallcher, L.M. and Sherman, W.R. (1980). „The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain”. J. Biol. Chem. 255: 10896-10901. PMID 6253491.
- ↑ Yoshikawa, T., Turner, G., Esterling, L.E., Sanders, A.R. and Detera-Wadleigh, S.D. (1997). „A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder”. Mol. Psychiatry 2: 393-397. PMID 9322233.
- ↑ 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.
- ↑ Ackermann, K.E., Gish, B.G., Honchar, M.P. and Sherman, W.R. (1987). „Evidence that inositol 1-phosphate in brain of lithium-treated rats results mainly from phosphatidylinositol metabolism”. Biochem. J. 242: 517-524. PMID 3036092.
Literatura
- 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.
Spoljašnje veze
- MeSH Inositol-phosphate+phosphatase
- p
- r
- u
Holinesteraza (Acetilholinesteraza, Butirilholinesteraza) • Pektinesteraza • 6-fosfoglukonolaktonaza • PAF acetilhidrolaza
Lipaza (Zavisna od žučnih soli, Gastrična/Lingvalna, Pankreasna, Lizozomalna, Hormon-sensitivna, Endotelna, Hepatička, Lipoproteinska, Monoacilglicerolna, Diacilglicerolna)
Fosfolipaza (A1, A2, B)Tioesteraza palmitoil proteina • Ubikvitin karboksilni-terminal hidrolaza L1
Alkalna fosfataza (ALPI, ALPL, ALPP) • Kiselinska fosfataza (Prostatična)/Tartrat-otporna kiselinska fosfataza/Fosfataze purpurne kiseline • Nukleotidaza • Glukoza 6-fosfataza • Fruktoza 1,6-bisfosfataza •
Kalcineurin • Fosfoproteinska fosfataza (PP2A) • OCRL • Piruvat dehidrogenazna fosfataza • Fruktoza 6-P,2-kinaza:fruktoza 2,6-bisfosfataza •PTEN • Fitaza • Inozitol-fosfat fosfataza (IMPA1)
Autotaksin • Fosfolipaza (C, D) • Sfingomijelin fosfodiesteraza (1) • PDE1 • PDE2 • PDE3 • PDE4A/PDE4B • PDE5 • Lecitinaza (Clostridium perfringens alfa toksin) • Fosfodiesteraza cikličnih nukleotida
arilsulfataza (Arilsulfataza A, Arilsulfataza B, Arilsulfataza E, Steroidna sulfataza) • Galaktozamine-6 sulfataza • Iduronat-2-sulfataza • N-acetilglukosamin-6-sulfataza
deoksiribonukleazu i
ribonukleazu)
3.1.11-16: Eksonukleaza |
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3.1.21-31: Endonukleaza |
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
