Characterization of a Site-specifically Modified Human Dihydrolipoamide Dehydrogenase Mutant Showing Significantly Changed Kinetic Properties

Journal of the Korean Chemical Society

article

Hakjung Kim¹ 

[1] Department of Chemistry, College of Natural and Life Sciences, Daegu University

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

DOI  :  10.5012/jkcs.2021.65.2.83

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 multifunctional homodimeric flavoenzyme (Fig. 1) with each subunit composed of 474 amino acids with a molecular mass of 50,216 daltons.1 E3 is an essential component in three α-keto acid dehydrogenase complexes (pyruvate, α-ketoglutarate and branched-chain α-keto acid dehydrogenase)2 and deoxidizes the dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of these dehydrogenase complexes. Patients with an E3 deficiency usually die young because an E3 deficiency is a fatal genetic defect that deteriorates the central nervous system, such as the brain, which leads to serious diseases including Leigh syndrome with permanent lactic acidaemia and mental retardation.

【 授权许可】

Unknown