Phenylalanine Hydroxylase Structure
Published by Anonymous on 2007/9/29 (3249 reads)
1: Hum Mutat. 1998;11(1):4-17.
In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function.
Waters PJ, Parniak MA, Nowacki P, Scriver CR.
Department of Pediatrics, McGill University, Montreal, Quebec, Canada.
Mutations in the human phenylalanine hydroxylase gene (PAH) altering the expressed cDNA nucleotide sequence (GenBank U49897) can impair activity of the corresponding enzyme product (hepatic phenylalanine hydroxylase, PAH) and cause hyperphenylalaninemia (HPA), a metabolic phenotype for which the major disease form is phenylketonuria (PKU; OMIM 261600). In vitro expression analysis of inherited human mutations in eukaryotic, prokaryotic, and cell-free systems is informative about the mechanisms of mutation effects on enzymatic activity and their predicted effect on the metabolic phenotype. Corresponding analysis of site-directed mutations in rat Pah cDNA has assigned critical functional roles to individual amino acid residues within the best understood species of phenylalanine hydroxylase. Data on in vitro expression of 35 inherited human mutations and 22 created rat mutations are reviewed here. The core data are accessible at the PAH Mutation Analysis Consortium Web site (http://www.mcgill.ca/pahdb).
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9450897 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Nat Struct Biol. 1997 Dec;4(12):995-1000.
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.
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.
Publication Types:
Comparative Study
Letter
Research Support, Non-U.S. Gov't
Review
PMID: 9406548 [PubMed - indexed for MEDLINE]
In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function.
Waters PJ, Parniak MA, Nowacki P, Scriver CR.
Department of Pediatrics, McGill University, Montreal, Quebec, Canada.
Mutations in the human phenylalanine hydroxylase gene (PAH) altering the expressed cDNA nucleotide sequence (GenBank U49897) can impair activity of the corresponding enzyme product (hepatic phenylalanine hydroxylase, PAH) and cause hyperphenylalaninemia (HPA), a metabolic phenotype for which the major disease form is phenylketonuria (PKU; OMIM 261600). In vitro expression analysis of inherited human mutations in eukaryotic, prokaryotic, and cell-free systems is informative about the mechanisms of mutation effects on enzymatic activity and their predicted effect on the metabolic phenotype. Corresponding analysis of site-directed mutations in rat Pah cDNA has assigned critical functional roles to individual amino acid residues within the best understood species of phenylalanine hydroxylase. Data on in vitro expression of 35 inherited human mutations and 22 created rat mutations are reviewed here. The core data are accessible at the PAH Mutation Analysis Consortium Web site (http://www.mcgill.ca/pahdb).
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9450897 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Nat Struct Biol. 1997 Dec;4(12):995-1000.
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.
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.
Publication Types:
Comparative Study
Letter
Research Support, Non-U.S. Gov't
Review
PMID: 9406548 [PubMed - indexed for MEDLINE]
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