Biochemical and biophysical approaches to characterization of the aromatic amino acid hydroxylases.
Methods Enzymol
; 704: 345-361, 2024.
Article
en En
| MEDLINE
| ID: mdl-39300655
ABSTRACT
The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase utilize a non-heme iron to catalyze the hydroxylation of the aromatic rings of their amino acid substrates, with a tetrahydropterin serving as the source of the electrons necessary for the monooxygenation reaction. These enzymes have been subjected to a variety of biochemical and biophysical approaches, resulting in a detailed understanding of their structures and mechanism. We summarize here the experimental approaches that have led to this understanding.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fenilalanina Hidroxilasa
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Methods Enzymol
Año:
2024
Tipo del documento:
Article
Pais de publicación:
Estados Unidos