Fig. 1: Schematic representation of the mitochondrial fatty acid synthesis (mtFAS) pathway, wild-type and engineered MECR and the reaction catalyzed by MECR/Etr1. | Nature Communications

Fig. 1: Schematic representation of the mitochondrial fatty acid synthesis (mtFAS) pathway, wild-type and engineered MECR and the reaction catalyzed by MECR/Etr1.

From: An engineered variant of MECR reductase reveals indispensability of long-chain acyl-ACPs for mitochondrial respiration

Fig. 1

a Schematic depiction of the mtFAS pathway. The indicated abbreviations (yeast (blue) /human (red)): Mct1/MCAT malonyl-CoA transferase, ACP acyl carrier protein, Cem1/OXSM 3-ketoacyl-ACP synthase, Oar1/KAR1 ketoacyl reductase, Htd2/HTD2 3-hydroxyacyl-thioester dehydratase, Etr1/MECR enoyl-thioester reductase, Lip5/LIAS lipoic acid synthetase. b Schematic representation of the wild-type and engineered MECR. The shown wild-type and engineered enzymes are liganded with C16- and C8-ACP molecules, respectively. The fatty acyl binding cavity extends from the catalytic site near the nicotinamide group of NADPH towards Ile129, which identifies the end of the cavity in the wild-type MECR. The engineered MECR mutant (shown as G165X) possesses a shortened substrate binding cavity discontinuing the synthesis of long-chain fatty acyl-ACP species by mtFAS. c MECR/Etr1 catalyzes the reduction of 2E-enoyl substrates to their saturated counterparts in a NADPH-dependent manner. MECR accepts fatty acyl groups that are attached to either CoA or ACP via a thioester bond.

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