We report the identification of two new 7-year-old patients with 3-hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency, a recently described inborn error of isoleucine metabolism. The defect is localized one step above 3-ketothiolase, resulting in a urinary metabolite pattern similar to that seen for deficiency of the latter. One patient has progressive neurodegenerative symptoms, whereas the clinical phenotype of the other patient is characterized by psychomotor retardation without loss of developmental milestones. A short-term biochemical response to an isoleucine-restricted diet was observed in both children.
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3-Hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency.
J Inherit Metab Dis
February 2004
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, USA.
A boy now 8 years old presented at 21 months of age with developmental arrest, followed by regression, cortical blindness and myoclonic seizures. Urine organic acid analysis revealed 3-hydroxy-2-methylbutyric acid and tiglyglycine; 3-ketothiolase enzyme activity was normal and he was subsequently found to have 3-hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency.
View Article and Find Full Text PDFClinical variability in 3-hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency.
Ann Neurol
May 2002
Metabolic Unit, University Children's Hospital, Freiburg, Germany.
We report the identification of two new 7-year-old patients with 3-hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency, a recently described inborn error of isoleucine metabolism. The defect is localized one step above 3-ketothiolase, resulting in a urinary metabolite pattern similar to that seen for deficiency of the latter. One patient has progressive neurodegenerative symptoms, whereas the clinical phenotype of the other patient is characterized by psychomotor retardation without loss of developmental milestones.
View Article and Find Full Text PDFShort-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: purification and characterization of a novel enzyme of isoleucine metabolism.
Arch Biochem Biophys
August 1995
Department of Chemistry, City College of the City University of New York, New York 10031, USA.
Short-chain L-3-hydroxy-2-methylacyl-CoA dehydrogenase (SC-HMAD), a soluble mitochondrial enzyme, was purified 6000-fold from rat liver in 6% yield by a six-step purification procedure. The purified enzyme was homogenous as judged by gel electrophoresis in the presence of sodium dodecyl sulfate. The molecular mass of this protein was estimated to be 28 kDa under denaturing conditions.
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