3wgt
From Proteopedia
Crystal structure of D-amino acid oxidase mutant
Structural highlights
FunctionOXDA_PIG Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. Publication Abstract from PubMedThe 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 alpha-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. Tailoring D-Amino Acid Oxidase from the Pig Kidney to R-Stereoselective Amine Oxidase and its Use in the Deracemization of alpha-Methylbenzylamine.,Yasukawa K, Nakano S, Asano Y Angew Chem Int Ed Engl. 2014 Mar 18. doi: 10.1002/anie.201308812. PMID:24644036[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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