An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity

Gideon James Grogan, Amina Frese, Sarah Barrass, Peter Sutton, Joe Adams

Research output: Contribution to journalArticlepeer-review


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 homolog of a PLP-dependent α-amino ε-caprolactam racemase (ACLR) from Ochrobactrum anthropi. We have determined the structure of this enzyme, OaACLR, to a resolution of 1.87 Å and 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.
Original languageEnglish
Pages (from-to)1-5
Number of pages5
Early online date10 Jul 2018
Publication statusE-pub ahead of print - 10 Jul 2018

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