Inozitol-1,4-bisfosfatna 1-fosfataza
| Inozitol-1,4-bisfosfatna 1-fosfataza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.3.57 | ||||||||
| CAS broj | 111694-13-4&title= 111070-17-8, 111694-13-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Inozitol-1,4-bisfosfatna 1-fosfataza (EC 3.1.3.57, inozitol-polifosfatna 1-fosfataza) je enzim sa sistematskim imenom 1D-mio-inozitol-1,4-bisfosfat 1-fosfohidrolaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 1D-mio-inozitol 1,4-bisfosfat + H2O 1D-mio-inozitol 4-fosfat + fosfat
Ovaj enzim deluje na inozitol 1,4-bisfosfat i inozitol 1,3,4-trisfosfat (formira inozitol 3,4-bisfosfat) sa sličnim Vmax vrednostima za oba supstrata.
Reference
- ↑ Berridge, M.J., Dawson, R.M.C., Downes, C.P., Heslop, J.P. and Irvine, R.F. (1983). „Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides”. Biochem. J. 212: 473-482. PMID 6309146.
- ↑ Connolly, T.M., Bansal, V.S., Bross, T.E., Irvine, R.F. and Majerus, P.W. (1987). „The metabolism of tris- and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes”. J. Biol. Chem. 262: 2146-2149. PMID 3029066.
- ↑ Inhorn, R.C. and Majerus, P.W. (1987). „Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+”. J. Biol. Chem. 262: 15946-15952. PMID 2824473.
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.
Spoljašnje veze
- MeSH Inositol-1,4-bisphosphate+1-phosphatase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
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
