Structural highlights
Publication Abstract from PubMed
The kinetic resolution of amino acid esters (AAEs) is a useful synthetic strategy for the preparation of single-enantiomer amino acids. The development of an enzymatic dynamic kinetic resolution (DKR) process for AAEs, which would give a theoretical yield of 100 % of the enantiopure product, would require an amino acid ester racemase (AAER); however, no such enzyme has been described. We have identified low AAER activity of 15 U mg(-1) in a homologue of a PLP-dependent alpha-amino -caprolactam racemase (ACLR) from Ochrobactrum anthropi. We have determined the structure of this enzyme, OaACLR, to a resolution of 1.87 A and, by using structure-guided saturation mutagenesis, in combination with a colorimetric screen for AAER activity, we have identified a mutant, L293C, in which the promiscuous AAER activity of this enzyme towards l-phenylalanine methyl ester is improved 3.7-fold.
An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity.,Frese A, Barrass SV, Sutton PW, Adams JP, Grogan G Chembiochem. 2018 Jun 13. doi: 10.1002/cbic.201800265. PMID:29897155[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Frese A, Barrass SV, Sutton PW, Adams JP, Grogan G. An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity. Chembiochem. 2018 Jun 13. doi: 10.1002/cbic.201800265. PMID:29897155 doi:http://dx.doi.org/10.1002/cbic.201800265
