Oleate hydratase catalyzes the hydration of a nonactivated carbon-carbon bond.
The hydration of oleic acid into 10-hydroxystearic acid was originally described for a Pseudomonas cell extract almost half a century ago. In the intervening years, the enzyme has never been characterized in any detail. We report here the isolation and characterization of oleate hydratase (EC 4.2.1.53) from Elizabethkingia meningoseptica.
Bevers
Loes E
LE
Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Pinkse
Martijn W H
MW
Verhaert
Peter D E M
PD
Hagen
Wilfred R
WR
D019840:2-Propanol / Q000494:pharmacology; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D041965:Flavobacteriaceae / Q000201:enzymology*; D006836:Hydro-Lyases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009829:Oleic Acids / Q000737:chemistry / Q000378:metabolism*; D012997:Solvents / Q000494:pharmacology; D013229:Stearic Acids / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D009829:Oleic Acids; D012997:Solvents; D013229:Stearic Acids; C070376:10-hydroxystearic acid; D006836:Hydro-Lyases; D019840:2-Propanol