3WGT

Crystal structure of D-amino acid oxidase mutant

Summary for 3WGT

• Entry DOI: 10.2210/pdb3wgt/pdb
• Descriptor: D-amino-acid oxidase, FLAVIN-ADENINE DINUCLEOTIDE, (1R)-1-phenylethanamine, ... (5 entities in total)
• Functional Keywords: oxidase, fad-binding, oxidoreductase
• Biological source: Sus scrofa (pig)
• Cellular location: Peroxisome: P00371
• Total number of polymer chains: 2
• Total formula weight: 80653.02

Authors

Yasukawa, K.,Nakano, S.,Asano, Y. (deposition date: 2013-08-09, release date: 2014-04-02, Last modification date: 2023-11-08)

Primary citation

Yasukawa, K.,Nakano, S.,Asano, Y.
Tailoring D-amino acid oxidase from the pig kidney to R-stereoselective amine oxidase and its use in the deracemization of alpha-methylbenzylamine.
Angew.Chem.Int.Ed.Engl., 53:4428-4431, 2014

PubMed Abstract: The deracemization of racemic amines to yield enantioenriched amines using S-stereoselective amine oxidases (AOx) has recently been attracting attention. However, R-stereoselective AOx that are suitable for deracemization have not yet been identified. An R-stereoselective AOx was now evolved from porcine kidney D-amino acid oxidase (pkDAO) and subsequently use for the deracemization of racemic amines. The engineered pkDAO, which was obtained by directed evolution, displayed a markedly changed substrate specificity towards R amines. The mutant enzyme exhibited a high preference towards the substrate α-methylbenzylamine and was used to synthesize the S amine through deracemization. The findings of this study indicate that further investigations on the structure-activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis.

PubMed: 24644036
DOI: 10.1002/anie.201308812

Experimental method

X-RAY DIFFRACTION (1.88 Å)