d-Amino acid oxidase is a FAD-dependent enzyme that catalyses the conversion of the d-enantiomer of amino acids into the corresponding α-keto acid. Substrate specificity of the enzyme from the yeast Rhodotorula gracilis was investigated towards aromatic amino acids, and particularly synthetic α-amino acids. A significant improvement of the activity (Vmax,app) and of the specificity constant (the Vmax,app/Km,app ratio) on a number of the substrates tested was obtained using a single-point mutant enzyme designed by a rational approach. With R. gracilis d-amino acid oxidase the complete resolution of d,l-homo-phenylalanine was obtained with the aim to produce the corresponding pure l-isomer and to use the corresponding α-keto acid as a precursor of the amino acid in the l-form.

Activity of yeast d-amino acid oxidase on aromatic unnatural amino acids

ROSINI, ELENA;MOLLA, GIANLUCA;POLLEGIONI, LOREDANO
2008

Abstract

d-Amino acid oxidase is a FAD-dependent enzyme that catalyses the conversion of the d-enantiomer of amino acids into the corresponding α-keto acid. Substrate specificity of the enzyme from the yeast Rhodotorula gracilis was investigated towards aromatic amino acids, and particularly synthetic α-amino acids. A significant improvement of the activity (Vmax,app) and of the specificity constant (the Vmax,app/Km,app ratio) on a number of the substrates tested was obtained using a single-point mutant enzyme designed by a rational approach. With R. gracilis d-amino acid oxidase the complete resolution of d,l-homo-phenylalanine was obtained with the aim to produce the corresponding pure l-isomer and to use the corresponding α-keto acid as a precursor of the amino acid in the l-form.
Caligiuri, A.; D'Arrigo, P.; Rosini, Elena; Pedrocchi fantoni, G.; Tessaro, D.; Molla, Gianluca; Servi, S.; Pollegioni, Loredano
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11383/1678399
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