Andrew M. Gulick

This study determines the structure of OaaC, a condensation domain involved in fatty acid amide biosynthesis, revealing how it occludes the ACP-binding site and is regulated by substrate-dependent oligomerization.

This study investigates the substrate selectivity of the FbsH adenylation domain in fimsbactin biosynthesis, identifying structural modifications that expand substrate tolerance and reveal downstream selectivity bottlenecks.

The paper determines the structure of the thioesterase domain of SulM and its complex with the upstream carrier protein domain, revealing a constrained active site for β-lactam formation.