Characterization of Two Site-Specific Mutations in Human Dihydrolipoamide Dehydrogenase Deteriorating the Apparent Enzyme Binding Affinities to Both Dihydrolipoamide and NAD +

Journal of the Korean Chemical Society

article

Hakjung Kim¹ 

[1] Department of Chemistry, College of Natural Science, Daegu University

关键词: Dihydrolipoamide dehydrogenase;    Pyridine nucleotide-disulfide oxidoreductase;    Flavoenzyme;   

DOI  :  10.5012/jkcs.2018.62.3.253

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Dihydrolipoamide dehydrogenase (E3) (dihydrolipoamide: NAD+ oxidoreductase; EC 1.8.1.4) is a homodimeric flavoenzyme containing one FAD as a prosthetic group at each subunit.1 E3 is a critical component in three α-keto acid dehydrogenase complexes (pyruvate, α-ketoglutarate, and branched-chain α-keto acid dehydrogenase complexes).2 E3 catalyzes the reoxidation of the dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of the three α-keto acid dehydrogenase complexes. Because E3 is an essential component in the three α-keto acid dehydrogenase, a decrease in E3 activity can affect the activities of all three complexes. E3 deficient patients typically die at an early age because an E3 deficiency is a critical genetic defect that affects the central nervous system. This can result in Leigh syndrome with recurrent episodes of hypoglycemia and ataxia, permanent lactic acidaemia and mental retardation.

【 授权许可】

Unknown