Fenilalanin 4-monooksigenaza
(преусмерено са Fenilalanin hidroksilaza)
| Fenilalanin 4-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| 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 | ||||||||
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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.
Reference
[уреди | уреди извор]- ^ 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 | уреди извор]- 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 | уреди извор]- Phenylalanine+4-monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
