Fenilalanin 4-monooksigenaza

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Fenilalanin 4-monooksigenaza
2pah.jpg
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 structures

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[uredi - уреди | uredi izvor]

  1. 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. 
  2. Kaufman, S. (1959). "Studies on the mechanism of the enzymic conversion of phenylalanine to tyrosine". J. Biol. Chem. 234: 2677–2682. PMID 14404870. 
  3. Mitoma, C. (1956). "Studies on partially purified phenylalanine hydroxylase". Arch. Biochem. Biophys. 60: 476–484. PMID 13292928. 
  4. Udenfriend, S. and Cooper, J.R. (1952). "The enzymic conversion of phenylalanine to tyrosine". J. Biol. Chem. 194: 503–511. PMID 14927641. 
  5. 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. 
  6. 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. 
  7. 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[uredi - уреди | uredi izvor]

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