Petkovic, H; Lill, RE; Sheridan, RM; Wilkinson, B; McCormick, EL; McArthur, HAI; ... Kendrew, SG; + view all Petkovic, H; Lill, RE; Sheridan, RM; Wilkinson, B; McCormick, EL; McArthur, HAI; Staunton, J; Leadlay, PF; Kendrew, SG; - view fewer (2003) A novel erythromycin, 6-desmethyl erythromycin D, made by substituting an acyltransferase domain of the erythromycin polyketide synthase. J ANTIBIOT , 56 (6) 543 - 551.
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The acyltransferase (AT) domain in module 4 of the erythromycin polyketide synthase (PKS) was substituted with an AT domain from the rapamycin PKS module 2 in order to alter the substrate specificity from methylmalonyl-CoA to malonyl-CoA. The resulting strain produced 6-desmethyl erythromycin D as the predominant product. This AT domain swap completes the library of malonyl-CoA AT swaps on the erythromycin PKS and reinforces PKS engineering as a robust and generic tool.
|Title:||A novel erythromycin, 6-desmethyl erythromycin D, made by substituting an acyltransferase domain of the erythromycin polyketide synthase|
|Keywords:||SUBSTRATE-SPECIFICITY, BIOSYNTHESIS, DERIVATIVES, FERMENTATION, HYDROXYLASE, ANTIBIOTICS, EXPRESSION|
|UCL classification:||UCL > School of Life and Medical Sciences > SLMS Planning and Performance Unit > SLMS Research Support Centre > Translational Research Office|
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