125356-61-8Relevant articles and documents
HheG, a halohydrin dehalogenase with activity on cyclic epoxides
Koopmeiners, Julia,Diederich, Christina,Solarczek, Jennifer,Vo?, Hauke,Mayer, Janine,Blankenfeldt, Wulf,Schallmey, Anett
, p. 6877 - 6886 (2017/11/06)
Halohydrin dehalogenases (HHDHs) are of biotechnological interest due to their promiscuous epoxide ring-opening activity with a set of negatively charged nucleophiles, enabling the formation of C-C, C-N, or C-O bonds. The recent discovery of HHDH-specific sequence motifs aided the identification of a large number of halohydrin dehalogenases from public sequence databases, enlarging the biocatalytic toolbox substantially. During the characterization of 17 representatives of these phylogenetically diverse enzymes, one HHDH, namely HheG from Ilumatobacter coccineus, was identified to convert cyclic epoxide substrates. The enzyme exhibits significant activity in the azidolysis of cyclohexene oxide and limonene oxide with turnover numbers of 7.8 and 44 s-1, respectively. As observed for other HHDHs, the cyanide-mediated epoxide ring-opening proceeded with lower rates. Wild-type HheG displays modest enantioselectivity, as the resulting azido- and cyanoalcohols of cyclohexene oxide ring-opening were obtained in 40% enantiomeric excess. These biocatalytic findings were further complemented by the crystal structure of the enzyme refined to 2.3 ?. Analysis of HheG's structure revealed a large open cleft harboring the active site. This is in sharp contrast to other known HHDH structures and aids in explaining the special substrate scope of HheG.
MCM-41 bound dibenzo-18-crown-6 ether: a recoverable phase-transfer nano catalyst for smooth and regioselective conversion of oxiranes to β-azidohydrins and β-cyanohydrins in water
Yousefi, Sarah,Kiasat, Ali Reza
, p. 92387 - 92393 (2015/11/16)
A new organic-inorganic hybrid nanocomposite was prepared by immobilizing dibenzo-18-crown-6 onto covalently linked amine functionalized mesoporous MCM-41 via a simple post-synthesis method. The heterogeneous hybrid nanocomposite was characterized by TEM,
Enzymatic resolution of trans-2-hydroxycyclohexanecarbonitrile in supercritical carbon dioxide
Utczás, Margita,Székely, Edit,Forró, Enik,Szllsy, áron,Fül?p, Ferenc,Simándi, Béla
body text, p. 3916 - 3918 (2011/08/09)
A novel, highly enantioselective (E ? 100) and environmentally benign method is presented for the kinetic resolution of trans-2- hydroxycyclohexanecarbonitrile in supercritical carbon dioxide. Using Candida antarctica Lipase B as a biocatalyst and vinyl a