Proteus myxofaciens

Turning to l-AAO, Pantaleone s industrial research group have reported" on the properties and use of an l-AAO from Proteus myxofaciens, overexpressed in Escherichia coli This l-AAO, unusually, appears not to produce H2O2 in the catalytic reaction, thus making the addition of catalase unnecessary. The enzyme has a broad specificity, with a preference for nonpolar amino acids. This l-AAO was used in conjunction with a D-amino acid transaminase (d-AAT) and an alanine racemase (AR) to allow an efficient conversion of L-amino acid in to D-amino acid (Scheme 4). 

Alexandre, F.-R., Pantaleone, D.P., Taylor, P.P., Fotheringham, I.G., Ager, D.J., and Turner, N.J. (2002) Amine-boranes effective reducing agents for the deracemisation of dl-amino acids using 1-amino acid oxidase from Proteus myxofaciens. Tetrahedron Lett., 43 (4), 707- 710. 

L-Amino Acids with l- -AAD Originating from Proteus myxofaciens in ... 

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