HSD17B8 and tuberculosis: FabG catalyzes reduction of beta-ketoacyl-acyl carrier (ACP) protein substrates by NADPH to beta-hydroxyacyl-ACP products, can also catalyze reduction of acetoacetyl-CoA, albeit less efficiently than paralog proteins, and appears to play a role in fatty acid synthesis.[48, 49] Initially characterized in E. coli, FabG1-4 orthologs are present in M. tuberculosis,[50] and some have been shown to be inhibited by isoniazid,[51] which is widely used in the treatment of tuberculosis.