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Hyperphenylalaninaemia caused by defects in biopterin metabolism
Author(s) -
Kaufman S.
Publication year - 1985
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01800655
Subject(s) - tetrahydrobiopterin , biopterin , phenylalanine hydroxylase , pterin , hyperphenylalaninemia , tyrosine , phenylalanine , biochemistry , tryptophan , tyrosine hydroxylase , cofactor , tryptophan hydroxylase , endocrinology , chemistry , biology , medicine , enzyme , amino acid , serotonin , receptor , serotonergic
The hepatic phenylalanine hydroxylating system consists of three essential components, phenylalanine hydroxylase, dihydropteridine reductase and the non‐protein coenzyme, tetrahydrobiopterin. The reductase and the pterin coenzyme are also essential components of the tyrosine and tryptophan hydroxylating systems. Recent studies have shown that there are three distinct forms of phenylketonuria or hyperphenylalaninaemia, each caused by the lack of one of these essential components. The variant forms of the disease that are caused by the lack of dihydropteridine reductase or tetrahydrobiopterin are characterized by severe neurological deterioration, impaired functioning of tyrosine and tryptophan hydroxylases and the resultant deficiency of tyrosine‐ and tryptophan‐derived monoamine neurotransmitters in brain.