Research

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


Reference:

Heath, C., Jeffries, A. C., Hough, D. W. and Danson, M. J., 2004. Discovery of the catalytic function of a putative 2-oxoacid dehydrogenase multienzyme complex in the thermophilic archaeon Thermoplasma acidophilum. FEBS Letters, 577 (3), pp. 523-527.

Related documents:

This repository does not currently have the full-text of this item.
You may be able to access a copy if URLs are provided below.

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.

Details

Item Type Articles
CreatorsHeath, C., Jeffries, A. C., Hough, D. W. and Danson, M. J.
DOI10.1016/j.febslet.2004.10.058
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code3968
Additional InformationID number: ISI:000225368300039

Export

Actions (login required)

View Item