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

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 alpha2beta2 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Heath C,Jeffries AC,Hough DW,Danson MJ

doi

10.1016/j.febslet.2004.10.058

keywords:

subject

Has Abstract

pub_date

2004-11-19 00:00:00

pages

523-7

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014579304013122

journal_volume

577

pub_type

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