4A6G

N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl methionine

Summary for 4A6G

• Entry DOI: 10.2210/pdb4a6g/pdb
• Related: 1SJA 1SJB 1SJC 1SJD
• Descriptor: N-ACYLAMINO ACID RACEMASE, N-ACETYLMETHIONINE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: lyase, biocatalysis
• Biological source: AMYCOLATOPSIS SP.
• Total number of polymer chains: 4
• Total formula weight: 158951.43

Authors

Baxter, S.,Royer, S.,Grogan, G.,Holt-Tiffin, K.E.,Taylor, I.N.,Fotheringham, I.G.,Campopiano, D.J. (deposition date: 2011-11-02, release date: 2012-11-14, Last modification date: 2023-12-20)

Primary citation

Baxter, S.,Royer, S.,Grogan, G.,Brown, F.,Holt-Tiffin, K.E.,Taylor, I.N.,Fotheringham, I.G.,Campopiano, D.J.
An Improved Racemase/Acylase Biotransformation for the Preparation of Enantiomerically Pure Amino Acids.
J.Am.Chem.Soc., 134:19310-, 2012

PubMed Abstract: Using directed evolution, a variant N-acetyl amino acid racemase (NAAAR G291D/F323Y) has been developed with up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids. The variant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic resolution which allows 98% conversion of N-acetyl-DL-allylglycine into D-allylglycine in 18 h at high substrate concentrations (50 g L(-1)). This is the first example of NAAAR operating under conditions which would allow it to be successfully used on an industrial scale for the production of enantiomerically pure α-amino acids. X-ray crystal analysis of the improved NAAAR variant allowed a comparison with the wild-type enzyme. We postulate that a network of novel interactions that result from the introduction of the two side chains is the source of improved catalytic performance.

PubMed: 23130969
DOI: 10.1021/JA305438Y

Experimental method

X-RAY DIFFRACTION (2.71 Å)