Fenilalanin 4-monooksigenaza
(Preusmjereno sa stranice Fenilalanin hidroksilaza)
| Fenilalanin 4-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.14.16.1 | ||||||||
| CAS broj | 9029-73-6 | ||||||||
| 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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Fenilalanin 4-monooksigenaza (EC 1.14.16.1, fenilalaninaza, fenilalaninska 4-hidroksilaza, fenilalaninska hidroksilaza) je enzim sa sistematskim imenom L-fenilalanin,tetrahidrobiopterin:kiseonik oksidoreduktaza (4-hidroksilacija).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-fenilalanin + tetrahidrobiopterin + O2 L-tirozin + 4a-hidroksitetrahidrobiopterin
Aktivni centar sadrži mononuklearno gvožđe(II). U reakciji učestvuje aren oksid koji se rearanžira i daje fenol hidroksilnu grupu.
- ↑ Guroff, G. and Rhoads, C.A. (1969). „Phenylalanine hydroxylation by Pseudomonas species (ATCC 11299a). Nature of the cofactor”. J. Biol. Chem. 244: 142-146. PMID 5773277.
- ↑ Kaufman, S. (1959). „Studies on the mechanism of the enzymic conversion of phenylalanine to tyrosine”. J. Biol. Chem. 234: 2677-2682. PMID 14404870.
- ↑ Mitoma, C. (1956). „Studies on partially purified phenylalanine hydroxylase”. Arch. Biochem. Biophys. 60: 476-484. PMID 13292928.
- ↑ Udenfriend, S. and Cooper, J.R. (1952). „The enzymic conversion of phenylalanine to tyrosine”. J. Biol. Chem. 194: 503-511. PMID 14927641.
- ↑ Carr, R.T., Balasubramanian, S., Hawkins, P.C. and Benkovic, S.J. (1995). „Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase”. Biochemistry 34: 7525-7532. PMID 7779797.
- ↑ Andersen, O.A., Flatmark, T. and Hough, E. (2001). „High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin”. J. Mol. Biol. 314: 266-278. PMID 11718561.
- ↑ Erlandsen, H., Kim, J.Y., Patch, M.G., Han, A., Volner, A., Abu-Omar, M.M. and Stevens, R.C. (2002). „Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates”. J. Mol. Biol. 320: 645-661. PMID 12096915.
- 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.