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Engineered biosynthesis of antiprotealide and other unnatural salinosporamide proteasome inhibitors.


ABSTRACT: A new shunt in the phenylalanine biosynthetic pathway to the nonproteinogenic amino acid L-3-cyclohex-2'-enylalanine was exploited in the marine bacterium Salinispora tropica by mutagenesis to allow for the genetic engineering of unnatural derivatives of the potent proteasome inhibitor salinosporamide A (2) such as antiprotealide (1).

SUBMITTER: McGlinchey RP 

PROVIDER: S-EPMC2814216 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Engineered biosynthesis of antiprotealide and other unnatural salinosporamide proteasome inhibitors.

McGlinchey Ryan P RP   Nett Markus M   Eustáquio Alessandra S AS   Asolkar Ratnakar N RN   Fenical William W   Moore Bradley S BS  

Journal of the American Chemical Society 20080531 25


A new shunt in the phenylalanine biosynthetic pathway to the nonproteinogenic amino acid L-3-cyclohex-2'-enylalanine was exploited in the marine bacterium Salinispora tropica by mutagenesis to allow for the genetic engineering of unnatural derivatives of the potent proteasome inhibitor salinosporamide A (2) such as antiprotealide (1). ...[more]

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