Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
The 2.0 A crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydroxylase. It provides the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria.
Erlandsen
H
H
Fusetti
F
F
Martinez
A
A
Hough
E
E
Flatmark
T
T
Stevens
R C
RC
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D003460:Crystallization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010651:Phenylalanine Hydroxylase / Q000737:chemistry* / Q000235:genetics; D010661:Phenylketonurias / Q000201:enzymology* / Q000235:genetics; D017510:Protein Folding; D014446:Tyrosine 3-Monooxygenase / Q000737:chemistry / Q000235:genetics
D010651:Phenylalanine Hydroxylase; D014446:Tyrosine 3-Monooxygenase