PAH:Fe2+ tetramer hydroxylates L-Phe to L-Tyr
L-Phe + BH4 + O2 → L-Tyr + 4aOH-BH4
- Reactome
- R-HSA-71118
- Compartment
- cytosol
- Rhea
- RHEA:20274
Inputs
- L-PheCHEBI:58095, C9H11NO2, cytosol
- BH4CHEBI:59560, C9H15N5O3, cytosol
- O2CHEBI:15379, O2, cytosol
Outputs
- L-TyrCHEBI:58315, C9H11NO3, cytosol
- 4aOH-BH4CHEBI:15642, C9H15N5O4, cytosol
Catalysed by
- phenylalanine 4-monooxygenase activity of PAH:Fe2+ tetramer [cytosol]EC 1.14.16.1
Literature
- Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation J Mol Biol, 2002
- Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J Biol Chem, 1998
- Phenylalanine hydroxylase deficiency in a population in Germany: mutational profile and nine novel mutations Hum Mutat, 1996