α-ケト酸の酸化分解を触媒するThiamin Diphosphate酵素に関する研究

概要

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In eukaryotic and prokaryotic cells it is well known that the 2-oxo acids are oxidized via CoA- and NAD^+-dependent and lipoic acid-mediated oxidative decarboxylation reaction by 2-oxo acid dehy drogenase multienzyme complex family, which composed of multiple copies of three component enzymes: TDP (thiamin diphosphate) -depenent α-keto acid dehydrogenase (E1), dihydrolipoamide acyltransferase (E2) and FAD-containing dihydrolipoamide dehydrogenase (E3). This paper focused on the biochemical and molecular biological characterization of porcine and human TDP-dependent pyruvate and 2-oxoglutarate dehydrogenases [E1p (α2β2) and E1o (α2)]. Human E1pα, E1pβ and E1o cDNAs and their genomic DNAs have been cloned and characterized their structural organiza tiOnS. The E1o gene mapped on chromosome 7p13-p14. The E1o promoter of 5'-flanking region lacked both canonical TATA and CAAT boxes, activated only by 2-oxoglutarate and contained two cis-acting elements, which bind to nuclear factor. Human E1p defect has been diagnosed by enzymatical analyses, immunoblotting and sequence analyses of PCR products of all exons of Elpot and β genes. A rapid and microquantitative method for analyses of 2-oxo acids in serum and urine has been estab lished and underwent clinical use successfully.
日本ビタミン学会の論文
2000-02-25