Title : The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme.

Pub. Date : 1999 Mar 5

PMID : 10037716






2 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons. ferric sulfate phenylalanine hydroxylase Homo sapiens
2 The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons. ferric sulfate phenylalanine hydroxylase Homo sapiens