Fenilalanin 4-monooksigenaza
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
| Fenilalanin 4-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.14.16.1 | ||||||||
| CAS broj | 9029-73-6 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 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.
Reference
уреди- ^ Guroff, G. & 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. & 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.
Literatura
уреди- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
уреди- Phenylalanine+4-monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
