4a6g | pdb_00004a6g

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

spinqualitylabelsall models 4a6g, resolution 2.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a6g is a 4 chain structure with sequence from Amycolatopsis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AME, MG Related: 1sjb, 1sja, 1sjc, 1sjd Activity: o-succinylbenzoate synthase, with EC number 4.2.1.113 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 alpha-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. An Improved Racemase/Acylase Biotransformation for the Preparation of Enantiomerically Pure Amino Acids.,Baxter S, Royer S, Grogan G, Brown F, Holt-Tiffin KE, Taylor IN, Fotheringham IG, Campopiano DJ J Am Chem Soc. 2012 Nov 15. PMID:23130969 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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