16899-08-4Relevant articles and documents
Biocatalytic study of novel oleate hydratases
Schmid, Jens,Steiner, Lisa,Fademrecht, Silvia,Pleiss, Jürgen,Otte, Konrad B.,Hauer, Bernhard
, p. S243 - S249 (2016)
The direct hydration of C[dbnd]C bonds to yield alcohols or the reverse dehydration is chemically challenging but highly sought after. Recently, oleate hydratases (OAHs) gained attention as biocatalytic alternatives capable of hydrating isolated, non-activated C[dbnd]C bonds. Their natural reaction is the conversion of oleic acid to (R)-10-hydroxystearic acid. In this work, we report the first comparative study of several OAHs. Therefore we established the Hydratase Engineering Database (HyED) comprising 2046 putative OAHs from eleven homologous families and selected nine homologs for cloning in E. coli. The heterologously expressed enzymes were evaluated concerning activity and substrate specificity. The enzymes have a broad substrate scope ranging from oleic acid (C18) to the novel synthetic substrate (Z)-undec-9-enoic acid (C11). The OAHs from Elizabethkingia meningoseptica and Chryseobacterium gleum showed the best expression, highest stability and broadest substrate scope, making them interesting candidates for directed evolution to engineer them for the application as general hydratase catalysts.
Controlling Chemoselectivity of Catalytic Hydroboration with Light
Bergamaschi, Enrico,Chen, Yi-Kai,Hohenadel, Melissa,Lunic, Danijela,McLean, Liam A.,Teskey, Christopher J.
, (2022/01/13)
The ability to selectively react one functional group in the presence of another underpins efficient reaction sequences. Despite many designer catalytic systems being reported for hydroboration reactions, which allow introduction of a functional handle fo
The CYPome of sorangium cellulosum so ce56 and identification of CYP109D1 as a new fatty acid hydroxylase
Khatri, Yogan,Hannemann, Frank,Ewen, Kerstin M.,Pistorius, Dominik,Perlova, Olena,Kagawa, Norio,Brachmann, Alexander O.,Mueller, Rolf,Bernhardt, Rita
experimental part, p. 1295 - 1305 (2011/09/20)
The first systematic study of the complete cytochrome P450 complement (CYPome) of Sorangium cellulosum So ce56, which is a producer of important secondary metabolites and has the largest bacterial genome sequenced to date, is presented. We describe the bioinformatic analysis of the So ce56 cytochrome P450 complement consisting of 21 putative P450 genes. Because fatty acids play a pivotal role during the complex life cycle of myxobacteria, we focused our studies on the characterization of fatty acid hydroxylases. Three novel potential fatty acid hydroxylases (CYP109D1, CYP264A1, and CYP266A1) were used for detailed characterization. One of them, CYP109D1 was able to perform subterminal hydroxylation of saturated fatty acids with the support of two autologous and one heterologous electron transfer system(s). The kinetic parameters for the product hydroxylation were derived.
