Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051873 | FEBS Letters | 2007 | 6 Pages |
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 (μmol mgâ1 minâ1) and Km value of 2.7 μM 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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Authors
Sara Tucci, William Martin,