The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates.
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 substrate loading. This observation has important implications for the engineering of biosynthetic pathways to produce polyketide products.
Sharma
Krishna K
KK
Department of Chemistry, Syracuse University, Syracuse, NY 13244-4100, USA.
Boddy
Christopher N
CN
D053898:Biosynthetic Pathways; D002384:Catalysis; D003543:Cysteamine / Q000031:analogs & derivatives*; D004917:Erythromycin / Q000031:analogs & derivatives / Q000096:biosynthesis*; D004952:Esters / Q000737:chemistry; D006868:Hydrolysis; D010866:Natamycin / Q000096:biosynthesis*; D048630:Polyketide Synthases / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013379:Substrate Specificity; D013457:Sulfur Compounds / Q000737:chemistry*; D013869:Thiolester Hydrolases / Q000737:chemistry* / Q000235:genetics
D004952:Esters; D011994:Recombinant Proteins; D013457:Sulfur Compounds; C034277:6-deoxyerythronolide B; D003543:Cysteamine; D004917:Erythromycin; D048630:Polyketide Synthases; D010866:Natamycin; D013869:Thiolester Hydrolases