Fenilalanin 4-monooksigenaza (EC1.14.16.1,fenilalaninaza,fenilalaninska 4-hidroksilaza,fenilalaninska hidroksilaza) jeenzim sa sistematskim imenomL-fenilalanin,tetrahidrobiopterin:kiseonik oksidoreduktaza (4-hidroksilacija).[1][2][3][4][5][6][7] Ovaj enzimkatalizuje sledećuhemijsku reakciju
- L-fenilalanin +tetrahidrobiopterin + O2
L-tirozin + 4a-hidroksitetrahidrobiopterin
Aktivni centar sadrži mononuklearnogvožđe(II). U reakciji učestvujearen oksid koji se rearanžira i dajefenol hidroksilnu grupu.
- ↑Guroff, G. and Rhoads, C.A. (1969). „Phenylalanine hydroxylation byPseudomonas 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 byChromobacterium 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.
