Open AccessA Novel Compound Heterozygous Tyrosine Hydroxylase Mutation (p.R441P) with Complex Phenotype
Author(s) -
Kristoffer Haugarvoll,
Laurence A. Bindoff
Publication year - 2011
Publication title -
journal of parkinson's disease/journal of parkinson's disease (online)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.747
H-Index - 45
eISSN - 1877-718X
pISSN - 1877-7171
DOI - 10.3233/jpd-2011-11006
Subject(s) - tyrosine hydroxylase , tetrahydrobiopterin , missense mutation , compound heterozygosity , dystonia , phenotype , phenylalanine hydroxylase , mutation , tyrosine , tyrosine 3 monooxygenase , gtp cyclohydrolase i , genetics , gene , enzyme , dopamine , biology , endocrinology , biochemistry , nitric oxide synthase , phenylalanine , amino acid , neuroscience
Tyrosine hydroxylase (TH) is a tetrahydrobiopterin (BH4) dependent enzyme that catalyses the conversion of L-tyrosine to L-dopa, the rate-limiting step in the biosynthesis of dopamine. Autosomal recessive mutations in the TH gene cause impaired TH activity and are associated with phenotypes ranging from autosomal recessive dopa-responsive dystonia (DRD) to progressive infantile encephalopathy. Herein, we present a patient with TH-deficiency due to two compound heterozygous missense mutations in the TH/gene, one of which is novel (p.R441P). A clinical update on TH-deficiency and clues on how to achieve a timely diagnosis of this highly treatable disorder is provided.