3 years ago

AibA/AibB Induces an Intramolecular Decarboxylation in Isovalerate Biosynthesis by Myxococcus xanthus

AibA/AibB Induces an Intramolecular Decarboxylation in Isovalerate Biosynthesis by Myxococcus xanthus
Christian Feiler, Wulf Blankenfeldt, Judith Hoffmann, Vlad Schütza, Tobias Bock, Eva Luxenburger, Rolf Müller
Isovaleryl coenzyme A (IV-CoA) is an important precursor for iso-fatty acids and lipids. It acts in the development of myxobacteria, which can produce this compound from acetyl-CoA through alternative IV-CoA biosynthesis (aib). A central reaction of aib is catalyzed by AibA/AibB, which acts as a cofactor-free decarboxylase despite belonging to the family of CoA-transferases. We developed an efficient expression system for AibA/AibB that allowed the determination of high-resolution crystal structures in complex with different ligands. Through mutational studies, we show that an active-site cysteine previously proposed to be involved in decarboxylation is not required for activity. Instead, AibA/AibB seems to induce an intramolecular decarboxylation by binding its substrate in a hydrophobic cavity and forcing it into a bent conformation. Our study opens opportunities for synthetic biology studies, since AibA/AibB may be suitable for the production of isobutene, a precursor of biofuels and chemicals. Based on structural and biochemical characterization of the unique cofactor-free decarboxylase AibA/AibB, an intramolecular decarboxylation mechanism supported by the geometry and hydrophobic character of the active site is proposed. This study opens up opportunities for synthetic biology approaches, since AibA/AibB is well suited to the bacterial production of isobutene, a precursor of renewable biofuels and chemicals.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201701992

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