EC Number   |
Reaction |
Reference |
|---|
    1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
1H-15N HSQC NMR spectra are obtained of the 15N-labeled protein alone and in the presence of phenylalanine. Regulatory domain of phenylalanine hydroxylase can bind phenylalanine, consistent with the presence of an allosteric site for the amino acid |
711021 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
analysis of conformational changes upon substrate binding |
657982 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
catalytic mechanism |
672057 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
enzyme requires an initial reduction of Cu2+ to Cu+ for activation |
438730 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
hydrogen/deuterium exchange monitored by mass spectrometry is used to gain insight into local conformational changes accompanying activation of rat phenylalanine hydroxylase by phenylalanine. Peptides in the regulatory and catalytic domains that lie in the interface between these two domains show large increases in the extent of deuterium incorporation from solvent in the presence of phenylalanine |
711233 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
kinetics, molecular dynamics simulations, structure-energetics calculations, and molecular interaction fields, structure-function analysis |
673511 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
mechansim, conformational transition and hysteresis |
657812 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
molecular mechanism |
686642 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
proposed catalytic cycle |
438755 |
| 1.14.16.1 | L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
residues S391 and G332 are important for activity |
673132 |
