The enzymes D-amino acid oxidase and glutaryl-7-ACAacylase (GA) are currently utilised for the industrial productionof 7-aminocephalosporanic acid (7-ACA, 2), an importantprecursor of semisyntetic cephalosporins. Specifically,GA is devoted to the cleavage of the amide bond betweenglutaric acid and 7-ACA in the intermediate glutaryl-7-ACA(1).The synthetic performances of this enzyme towards 1have been widely investigated, while very little is known onGA substrate specificity.We have found that an industrial GAis very specific for the acyl moiety that has to be released, theglutaryl derivatives being by far the best substrates. On theother hand, this enzyme accepts a wide variety of “leavinggroups”. Not only N-glutarate of b-lactam derivatives, butalso N-glutaryl aminoacids as well as N-glutarylamides (aromaticand aliphatic) could be hydrolysed by GA, which, additionally,showed a significant esterase activity. Morenotably, GA-catalysed hydrolyses were highly enantioselective
Glutaryl-7-ACA acylase: a new tool for the biocatalyzed kinetic resolution of racemic amines and alcohols / Raimondi, Stefano; Forti, Luca; D., Monti; S., Riva. - In: CHEMICKÉ LISTY. - ISSN 0009-2770. - STAMPA. - 97:(2003), pp. 418-419. (Intervento presentato al convegno 6th International Symposium on Biocatalysis and Biotransformations - BIOTRANS 2003 tenutosi a Olomouc (Repubblica Ceca) nel 28 giugno - 3 luglio 2003).
Glutaryl-7-ACA acylase: a new tool for the biocatalyzed kinetic resolution of racemic amines and alcohols
RAIMONDI, Stefano;FORTI, Luca;
2003
Abstract
The enzymes D-amino acid oxidase and glutaryl-7-ACAacylase (GA) are currently utilised for the industrial productionof 7-aminocephalosporanic acid (7-ACA, 2), an importantprecursor of semisyntetic cephalosporins. Specifically,GA is devoted to the cleavage of the amide bond betweenglutaric acid and 7-ACA in the intermediate glutaryl-7-ACA(1).The synthetic performances of this enzyme towards 1have been widely investigated, while very little is known onGA substrate specificity.We have found that an industrial GAis very specific for the acyl moiety that has to be released, theglutaryl derivatives being by far the best substrates. On theother hand, this enzyme accepts a wide variety of “leavinggroups”. Not only N-glutarate of b-lactam derivatives, butalso N-glutaryl aminoacids as well as N-glutarylamides (aromaticand aliphatic) could be hydrolysed by GA, which, additionally,showed a significant esterase activity. Morenotably, GA-catalysed hydrolyses were highly enantioselective
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