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. 2007 Apr 17;581(8):1561-6.
doi: 10.1016/j.febslet.2007.03.013. Epub 2007 Mar 15.

A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola

Sara Tucci  1 , William Martin
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Free article

A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola

Sara Tucci et al. FEBS Lett. .
Free article

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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