Petkovic Hrvoje, Lill Rachel E, Sheridan Rose M, Wilkinson Barrie, McCormick Ellen L, McArthur Hamish A I, Staunton James, Leadlay Peter F, Kendrew Steven G
Biotica Technology Limited, 181 A Huntingdon Road, Cambridge CB3 0DJ, UK.
J Antibiot (Tokyo). 2003 Jun;56(6):543-51. doi: 10.7164/antibiotics.56.543.
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.
为了将底物特异性从甲基丙二酰辅酶A改变为丙二酰辅酶A,红霉素聚酮合酶(PKS)模块4中的酰基转移酶(AT)结构域被雷帕霉素PKS模块2中的AT结构域所取代。所得菌株产生6-去甲基红霉素D作为主要产物。这种AT结构域的交换完成了红霉素PKS上丙二酰辅酶A-AT交换文库,并强化了PKS工程作为一种强大且通用的工具。