The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates

KK Sharma, CN Boddy

Index: Sharma, Krishna K.; Boddy, Christopher N. Bioorganic and Medicinal Chemistry Letters, 2007 , vol. 17, # 11 p. 3034 - 3037

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Citation Number: 37

Abstract

The recombinant polyketide synthase thioesterase domains from the pimaricin and 6- deoxyerythronolide B biosynthetic pathways catalyze hydrolysis of a number of simple N- acetylcysteamine thioester derivatives. This study demonstrates that thioesterases are not highly substrate selective in formation of the acyl-enzyme intermediate, in contrast to non- ribosomal peptide synthase thioesterase domains that show very high specificity for ...