1722-95-8Relevant articles and documents
A practical preparation of (R)- and (S)-N-Boc-2-methylpiperidines
Doller, Dario,Davies, Robert,Chackalamannil, Samuel
, p. 1275 - 1278 (1997)
The resolution of (±)-2-methylpiperidine using D- and L-tartaric acid followed by direct conversion of the intermediate tartrate salts to (R) and (S)-N-Boc-2-methylpiperidine is described. Also described is an NMR protocol for assessing the optical purity of the intermediate tartrate salts as well as the free bases. The resolved enantiomers showed an ee of >98% based on NMR integration.
Role of Methanol in Chiral Combinations of Host-Guest Molecules in the Inclusion Crystal: Structure Determination by X-Ray Crystallography
Toda, Fumio,Tanaka, Koichi,Miyahara, Ikuko,Akutsu, Shohei,Hirotsu, Ken
, p. 1795 - 1796 (1994)
(S,S)-(-)-1,4-bisbenzene (2) and (S,S)-(-)-9,10-bisanthracene (3) include one enantiomer of racemic guest compound when the complexation is carried out in toluene, but include the other enantiomer and MeOH in a 1:1:1 ratio when the complexation is carried out in MeOH; the X-ray crystal structure of a 1:1:1 complex of 3, (S)-(+)-2-methylpiperidine and MeOH is reported, and preparation of the new chiral host compound (3) is also described.
Continuous Flow Chiral Amine Racemization Applied to Continuously Recirculating Dynamic Diastereomeric Crystallizations
Kwan, Maria H. T.,Breen, Jessica,Bowden, Martin,Conway, Louis,Crossley, Ben,Jones, Martin F.,Munday, Rachel,Pokar, Nisha P. B.,Screen, Thomas,Blacker, A. John
, p. 2458 - 2473 (2021/02/06)
A new, dynamic diastereomeric crystallization method has been developed, in which the mother liquors are continuously separated, racemized over a fixed-bed catalyst, and recirculated to the crystallizer in a resolution-racemization-recycle (R3) process. S
Sequence-Based In-silico Discovery, Characterisation, and Biocatalytic Application of a Set of Imine Reductases
Velikogne, Stefan,Resch, Verena,Dertnig, Carina,Schrittwieser, Joerg H.,Kroutil, Wolfgang
, p. 3236 - 3246 (2018/08/03)
Imine reductases (IREDs) have recently become a primary focus of research in biocatalysis, complementing other classes of amine-forming enzymes such as transaminases and amine dehydrogenases. Following in the footsteps of other research groups, we have established a set of IRED biocatalysts by sequence-based in silico enzyme discovery. In this study, we present basic characterisation data for these novel IREDs and explore their activity and stereoselectivity using a panel of structurally diverse cyclic imines as substrates. Specific activities of >1 U/mg and excellent stereoselectivities (ee>99 %) were observed in many cases, and the enzymes proved surprisingly tolerant towards elevated substrate loadings. Co-expression of the IREDs with an alcohol dehydrogenase for cofactor regeneration led to whole-cell biocatalysts capable of efficiently reducing imines at 100 mM initial concentration with no need for the addition of extracellular nicotinamide cofactor. Preparative biotransformations on gram scale using these ‘designer cells’ afforded chiral amines in good yield and excellent optical purity.