Recombinant whole-cell mediated baeyer-villiger oxidation of perhydropyran-type ketones.
Recombinant Escherichia coli cells expressing eight Baeyer-Villiger monooxygenases of bacterial origin have been utilized to oxidize prochiral heterocyclic ketones containing a pyran ring system. Within the biotransformation, two stereogenic centers were introduced with high control of enantioselectivity. The chemoselectivity of the enzymatic reaction was found to be high in favor of the Baeyer-Villiger process when using substituted ketone precursors incorporating functional groups labile to oxidation. A significantly different behavior was observed for two groups of monooxygenases with respect to substrate acceptance, which is consistent with our previous classification into two enzyme clusters.
Mihovilovic
Marko D
MD
Vienna University of Technology, Institute of Applied Synthetic Chemistry, Getreidemarkt 9/163-OC, A-1060 Vienna. mmihovil@pop.tuwien.ac.at
Grötzl
Birgit
B
Kandioller
Wolfgang
W
Muskotál
Adél
A
Snajdrova
Radka
R
Rudroff
Florian
F
Spreitzer
Helmut
H
D001711:Biotransformation; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007659:Ketones / Q000737:chemistry / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011714:Pyrans / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013237:Stereoisomerism
D007659:Ketones; D011714:Pyrans; D011994:Recombinant Proteins; D006899:Mixed Function Oxygenases