Pathways & interactions
Literature: Aromatic amino acid hydroxylase (IPR001273)
References used in this entry
The following publications were referred to in the abstract:
Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC.
Nat. Struct. Biol. 4 995-1000 1997
PMID: 9406548 Related citations
Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases.
Grenett HE, Ledley FD, Reed LL, Woo SL.
Proc. Natl. Acad. Sci. U.S.A. 84 5530-4 1987
PMID: 3475690 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.
Andersen OA, Stokka AJ, Flatmark T, Hough E.
J. Mol. Biol. 333 747-57 2003
PMID: 14568534 Related citations
Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.
Erlandsen H, Pey AL, Gamez A, Perez B, Desviat LR, Aguado C, Koch R, Surendran S, Tyring S, Matalon R, Scriver CR, Ugarte M, Martinez A, Stevens RC.
Proc. Natl. Acad. Sci. U.S.A. 101 16903-8 2004
PMID: 15557004 Related citations
Crystal structure of tryptophan hydroxylase with bound amino acid substrate.
Windahl MS, Petersen CR, Christensen HE, Harris P.
Biochemistry 47 12087-94 2008
PMID: 18937498 Related citations
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.
Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC.
Biochemistry 41 12569-74 2002
PMID: 12379098 Related citations
Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability.
Leiros HK, Pey AL, Innselset M, Moe E, Leiros I, Steen IH, Martinez A.
J. Biol. Chem. 282 21973-86 2007
PMID: 17537732 Related citations