Discovery of the catalytic function of a putative 2-oxoacid dehydrogenase multienzyme complex in the thermophilic archaeon Thermoplasma acidophilum

C Heath, A C Jeffries, D W Hough, M J Danson

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Those aerobic archaea whose genomes have been sequenced possess a single 4-gene operon that, by sequence comparisons with Bacteria and Eukarya, appears to encode the three component enzymes of a 2-oxoacid dehydrogenase multienzyme complex. However, no catalytic activity of any such complex has ever been detected in the Archaea. In the current paper, we have cloned and expressed the first two genes of this operon from the thermophilic archaeon, Thermoplasma acidophilum. We demonstrate that the protein products form an alpha(2)beta(2) hetero-tetramer possessing the decarboxylase catalytic activity characteristic of the first component enzyme of a branched-chain 2-oxoacid dehydrogenase multienzyme complex. This represents the first report of the catalytic function of these putative archaeal multienzyme complexes. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Original languageEnglish
Pages (from-to)523-527
Number of pages5
JournalFEBS Letters
Volume577
Issue number3
DOIs
Publication statusPublished - 2004

Fingerprint Dive into the research topics of 'Discovery of the catalytic function of a putative 2-oxoacid dehydrogenase multienzyme complex in the thermophilic archaeon Thermoplasma acidophilum'. Together they form a unique fingerprint.

  • Cite this