The Structure of a Ketored the Organization of the b-C Enzymes of Modular Polyk

b-keto group formed after each condensation: KR uses the ‘‘KR’ ’ region always appear together and are present NADPH to stereospecifically reduce it to a hydroxyl group, DH removes the hydroxyl group to create a dou-ble bond, and ER uses NADPH to reduce the double bond. In this way, a methylene functionality is produced by a complete module, which contains each of these en-zyme activities. To create a more functionalized ketide in greater than 95 % of the modules. In a full module, they border DH, ER, and ACP. Hybrid synthases containing a KR replacement have only been successful when the large interdomain linker was included, yet its function was unclear (Bedford et al., 1996; McDaniel et al., 1997). In limited proteolysis experiments of DEBS1