Literature DB >> 3342049

Properties of component X of rat heart pyruvate dehydrogenase complex.

S Matuda1, K Nakano, I Tabata, S Matuo, T Saheki.   

Abstract

Pyruvate dehydrogenase complex was purified from rat heart. A new component(mol.wt; 52,000) was found in the purified complex in addition to well known three component enzymes. This component(referred to as component X) was acetylated with [2-14C] pyruvate in the absence of CoA as well as lipoate acetyltransferase. The anti-lipoate acetyltransferase antibody reacted with component X and lipoate acetyltransferase, suggesting that component X shows homology with lipoate acetyltransferase in protein structure. cDNA for lipoate acetyltransferase was isolated from rat liver cDNA library in lambda gt 11. cDNA for lipoate acetyltransferase recognized two kinds of mRNAs of 3.5 Kb and 2.5 Kb.

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Year:  1988        PMID： 3342049     DOI： 10.1016/0006-291x(88)90464-0

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  2 in total

1.  Reconstitution of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes: analysis of protein X involvement and interaction of homologous and heterologous dihydrolipoamide dehydrogenases.

Authors:  S J Sanderson; S S Khan; R G McCartney; C Miller; J G Lindsay
Journal:  Biochem J       Date:  1996-10-01       Impact factor: 3.857

2.  Defects in the E2 lipoyl transacetylase and the X-lipoyl containing component of the pyruvate dehydrogenase complex in patients with lactic acidemia.

Authors:  B H Robinson; N MacKay; R Petrova-Benedict; I Ozalp; T Coskun; P W Stacpoole
Journal:  J Clin Invest       Date:  1990-06       Impact factor: 14.808
  2 in total

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