A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola.
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.
Tucci
Sara
S
Institute of Botany III, Heinrich-Heine University of Duesseldorf, Universitaetsstrasse 1, 40225 Duesseldorf, Germany. sara.tucci@uni-duesseldorf.de <sara.tucci@uni-duesseldorf.de>
Martin
William
W
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002384:Catalysis; D003001:Cloning, Molecular; D005227:Fatty Acids / Q000096:biosynthesis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D048373:Treponema denticola / Q000201:enzymology*
D001426:Bacterial Proteins; D005227:Fatty Acids; D011994:Recombinant Proteins; D044925:Oxidoreductases Acting on CH-CH Group Donors; C434934:trans-2-enoyl-CoA reductase (NADPH); D009247:NADH, NADPH Oxidoreductases