Fosforilaza
Fosforilaza (EC 2.4.1.1, mišićna fosforilaza a i b, amilofosforilaza, polifosforilaza, amilopektinska fosforilaza, glukanska fosforilaza, alfa-glukanska fosforilaza, 1,4-alfa-glukanska fosforilaza, glukozanska fosforilaza, glikogenska fosforilaza, granulozna fosforilaza, maltodekstrinska fosforilaza, mišićna fosforilaza, miofosforilaza, fosforilaza krompira, skrobna fosforilaza, 1,4-alfa-D-glukan:fosfat alfa-D-glukoziltransferaza) je enzim sa sistematskim imenom (1->4)-alfa-D-glukan:fosfat alfa-D-glukoziltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Fosforilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| Identifikatori | |||||||||
| EC broj | 2.4.1.1 | ||||||||
| CAS broj | 9035-74-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- [(1->4)-alfa-D-glukozil]n + fosfat [(1->4)-alfa-D-glukozil]n-1 + alfa-D-glukoza 1-fosfat
Prirodni supstrati su između ostalog maltodekstrin fosforilaza, skrob fosforilaza, i glikogen fosforilaza.
Reference uredi
- ↑ Baum, H. and Gilbert, G.A. (1953). „A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme”. Nature 171: 983-984. PMID 13063502.
- ↑ Chen, G.S. and Segel, I.H. (1968). „Purification and properties of glycogen phosphorylase from Escherichia coli”. Arch. Biochem. Biophys. 127: 175-186. PMID 4878695.
- ↑ Cowgill, R.W. (1959). „Lobster muscle phosphorylase: purfication and properties”. J. Biol. Chem. 234: 3146-3153. PMID 13812491.
- ↑ Fischer, E.H., Pocker, A. and Saari, J.C. (1970). „The structure, function and control of glycogen phosphorylase”. u: Campbell, P.N. and Greville, G.D.. Essays in Biochemistry. 6. London and New York: Academic Press. str. 23-68.
- ↑ Green, A.A. and Cori, G.T. (1943). „Crystalline muscle phosphorylase. I. Preparation, properties, and molecular weight”. J. Biol. Chem. 151: 21-29.
- ↑ Hanes, C.S. (1940). „The breakdown and synthesis of starch by an enzyme from pea seeds”. Proc. R. Soc. Lond. B Biol. Sci. 128: 421-450.
Literatura uredi
- 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.
- Fischer, E.H., Pocker, A. and Saari, J.C. (1970). „The structure, function and control of glycogen phosphorylase”. u: Campbell, P.N. and Greville, G.D.. Essays in Biochemistry. 6. London and New York: Academic Press. str. 23-68.