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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola
1Institute of Botany III, Heinrich-Heine University of Duesseldorf, Universitaetsstrasse 1, 40225 Duesseldorf, Germany. sara.tucci@uni-duesseldorf.de <sara.tucci@uni-duesseldorf.de>
Abstract:
An NADH-dependent trans-2-enoyl-CoA reductase (EC1.1.1.36) from the Gram negative spirochete Treponema denticola was identified, expressed and biochemically characterized. The recombinant protein is a monomeric enzyme with a molecular mass of 44 kDa with a specific activity of 43+/-4.8 U/mg (micromol mg(-1)min(-1)) and K(m) value of 2.7 microM for crotonoyl-CoA. This NADH-dependent trans-2-enoyl-CoA reductase represents the first enzymatically characterized member of a prokaryotic protein family involved in a fatty acid synthesis pathway that is distinct from the familiar fatty acid synthase system.
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