In parallel to the activity for customers and our participation in funded international or european research projects , at Biochemize we are developing our own research lines, focused on the development of enzymatic tools for carboligations and hydroxylations, and the generation of our own libraries of lipases and estearases.
Besides, Biochemize has made an active collaboration in the publication Engineered l-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of a,a-Dialkyl-a-Amino Acids, on Angewandte Chemie. Here, you can take a look to the abstract:
a,a-Disubstituted a-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5’-phosphate (PLP)-dependent l-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth ; EC 126.96.36.199) was engineered to achieve the stereoselective synthesis of a broad structural variety of a,a-dialkyl-a-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids d-Ala and d-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.
For more information, check out http://www.ncbi.nlm.nih.gov/pubmed/25611820#.