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A novel prokaryotic trans ‐2‐enoyl‐CoA reductase from the spirochete Treponema denticola
Author(s) -
Tucci Sara,
Martin William
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.013
Subject(s) - treponema denticola , treponema , microbiology and biotechnology , reductase , chemistry , biology , biochemistry , bacteria , enzyme , virology , genetics , porphyromonas gingivalis , syphilis , human immunodeficiency virus (hiv)
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 mg −1 min −1 ) and K m 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.