Novel (S)-Selective Hydrolase from Arthrobacter sp. K5 for Kinetic Resolution of Cyclic Amines

Chiral 2-methylpiperidine (2-MPI) is an important building block that has potential for applications in pharmaceuticals and pesticides. In this study, we observed the hydrolase Arthrobacter sp. K5 exhibits high (S)-selectivity toward rac-N-pivaloyl-2-MPI to yield (S)-2-MPI with 80.2% enantiomeric excess (ee) a 38.2% conversion. The hydrolase, which was identified by analyses of partial amino acid sequences purified enzyme genome sequence K5, exhibited moderate homology amidohydrolases up 67% (molinate from Gulosibacter molinativorax). gene overexpressed Rhodococcus erythropolis. recombinant cells produced 83.5% ee 48.4% conversion (E = 26.3) 100 mM rac-N-pivaloyl-2-MPI. These results suggest possibility efficient preparation chiral 2-MPI kinetic resolution.