Journal article
Structural basis for disulphide-CoA inhibition of a butyryl-CoA hexameric thioesterase
Y Khandokar, P Srivastava, S Raidal, S Sarker, JK Forwood
Journal of Structural Biology | Published : 2020
Abstract
Acyl-coenzyme A thioesterases (ACTs) catalyse the hydrolysis of thioester bonds between fatty-acyl chains and coenzyme A (CoA), producing a free fatty-acyl chain and CoA. These enzymes are expressed ubiquitously across prokaryotes and eukaryotes, and play important roles in lipid metabolism. There are 25 thioesterase families, subdivided based on their active site configuration, protein oligomerization, and substrate specificity. Understanding the mechanism of regulation within these families is important due to their roles in controlling the cell concentration of a range of fatty acids and CoA-bound compounds. Here we report a structural basis for a novel mode of inhibition of an ACT from S..
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Funding Acknowledgements
The research in the authors' laboratories has been supported by Australian Research Council grant, Y.K. is supported by Charles Shirt University COMPACT scholarship, P.S. is supported by Charles Shirt University PRS scholarship, J.K.F is supported by Australian Research Council Future Fellowship. S.S. is funded by the Discovery Early Career Researcher Award of the Australian Research Council. We acknowledge the use of the Australian Synchrotron and help of Australian Synchrotron staff in the data collection. This research was undertaken in part using the MX2 beamline at the Australian Synchrotron, part of ANSTO, and made use of the Australian Cancer Research Foundation (ACRF) detector.