Pyruvate dehydrogenase E3 binding protein deficiency.

Abstract

Primary defects of the E3 binding protein component of the pyruvate dehydrogenase complex appear to be a rare cause of pyruvate dehydrogenase deficiency. We describe two new, unrelated patients with mutations in the E3 binding protein gene, in both cases involving the conserved dinucleotides of splice junctions. Both patients presented with delayed development and lactic acidosis, features that are also found in patients with the more common pyruvate dehydrogenase E1 alpha subunit deficiency; however, they both had significant residual enzyme activity in cultured fibroblasts and prolonged survival.

• Authors: Ruth M Brown, Rosie A Head, Garry K Brown
• Journal: Human genetics (Hum Genet) Vol. 110 Issue 2 Pg. 187-91 (Feb 2002) ISSN: 0340-6717 [Print] Germany
• PMID: 11935326 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• PDHX protein, human
• Peptides
• Pyruvate Dehydrogenase Complex
• RNA, Messenger
• Pyruvate Dehydrogenase (Lipoamide)

Topics

• Adolescent
• Base Sequence
• Cells, Cultured
• Child
• Consanguinity
• Female
• Fibroblasts (enzymology, pathology)
• Humans
• Male
• Peptides (deficiency, genetics)
• Pyruvate Dehydrogenase (Lipoamide) (genetics)
• Pyruvate Dehydrogenase Complex (genetics)
• RNA, Messenger (genetics)
• Reverse Transcriptase Polymerase Chain Reaction
• Transcription, Genetic