6GIO

Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi

Summary for 6GIO

• Entry DOI: 10.2210/pdb6gio/pdb
• Descriptor: Amino acid amide racemase, PYRIDOXAL-5'-PHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: plp, isomerase, amino acid, amino acid amide, amino acid ester, racemase
• Biological source: Ochrobactrum anthropi
• Total number of polymer chains: 4
• Total formula weight: 188500.78

Authors

Frese, A.,Grogan, G. (deposition date: 2018-05-14, release date: 2019-03-27, Last modification date: 2024-01-17)

Primary citation

Frese, A.,Barrass, S.V.,Sutton, P.W.,Adams, J.P.,Grogan, G.
An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity.
Chembiochem, 2018

PubMed Abstract: 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 in a homologue 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, 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.

PubMed: 29897155
DOI: 10.1002/cbic.201800265

Experimental method

X-RAY DIFFRACTION (1.87 Å)