Related Experiment Video
Updated: Aug 15, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage
J Cortes1, K E Wiesmann, G A Roberts
1Cambridge Centre for Molecular Recognition, University of Cambridge, UK.
Abstract:
Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension. The resulting mutant markedly accelerates formation of the predicted triketide lactone, compared to a control in which the repositioned domain is inactive. Repositioning of the cyclase should be generally useful for redirecting polyketide synthesis to obtain polyketides of specified chain lengths.
Related Concept Videos
Mismatch Repair
Ligand Binding and Linkage
DNA Topoisomerases
Types and Mechanism of action
Topoisomerases are divided into two main types. Type I...
Long-patch Base Excision Repair
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
Mismatch Repair
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...

