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Characterization of a point mutation in the pyruvate dehydrogenase E1α gene from two boys with primary lactic acidaemia
Author(s) -
Awata H.,
Endo F.,
Tanoue A.,
Kitano A.,
Matsuda I.
Publication year - 1994
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/bf00711616
Subject(s) - pyruvate dehydrogenase complex , glutamine , point mutation , serine , biochemistry , biology , mutation , arginine , lactic acid , amino acid , protein subunit , phosphorylation , genetics , gene , enzyme , bacteria
Summary We report here a novel mutation in the codon for amino acid 263 resulting in the change from arginine to glutamine in the pyruvate dehydrogenase (PDH) E1α gene, in two boys with primary lactic acidaemia, from independent families. The mutation changes an amino acid located between the two serine residues which are the sites of phosphorylation of the subunit protein. In one family, the mutation was de novo and in the other it was transmitted from mother to son. The amino acid substitution may affect function of the PDH complex via phosphorylation and dephosphorylation of the E1α subunit. Derangement in the regulation of activity of the PDH complex may explain the primary lactic acidaemia in the patients.