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Stenotrophomonas maltophilia OleC‐Catalyzed ATP‐Dependent Formation of Long‐Chain Z ‐Olefins from 2‐Alkyl‐3‐hydroxyalkanoic Acids
Author(s) -
Kancharla Papireddy,
Bonnett Shilah A.,
Reynolds Kevin A.
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600063
Subject(s) - stenotrophomonas maltophilia , alkyl , catalysis , chemistry , stenotrophomonas , long chain , organic chemistry , medicinal chemistry , biochemistry , bacteria , biology , pseudomonas aeruginosa , polymer science , genetics , 16s ribosomal rna , gene
The bacterial pathway of olefin biosynthesis starts with OleA catalyzed “head‐to‐head” condensation of two CoA‐activated long‐chain fatty acids to generate ( R )‐2‐alkyl‐3‐ketoalkanoic acids. A subsequent OleD‐catalyzed reduction generates (2 R ,3 S )‐2‐alkyl‐3‐hydroxyalkanoic acids. We now show that the final step in the pathway is an OleC‐catalyzed ATP‐dependent decarboxylative dehydration to form the corresponding Z olefins. Higher k cat /K m values were seen for substrates with longer alkyl chains. All four stereoisomers of 2‐hexyl‐3‐hydroxydecanoic acid were shown to be substrates, and GC‐MS and NMR analyses confirmed that the product in each case was ( Z )‐pentadec‐7‐ene. LC‐MS analysis supported the formation of AMP adduct as an intermediate. The enzymatic and stereochemical course of olefin biosynthesis from long‐chain fatty acids by OleA, OleD and OleC is now established.