InterPro domain: IPR014358

This entry contains enoyl-[acyl-carrier-protein] reductases ( 1.3.1.9 ). They are components of the type II (dissociable) fatty acid synthase system and catalyse the terminal reaction in the fatty acid elongation cycle.

They belong to the short-chain dehydrogenases/reductases (SDR) domain superfamily [ 1 , 2 , 3 ]. Crystal structures of these proteins have been extensively studied [ 4 , 5 , 6 , 7 , 8 , 9 , 10 ].

1. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34, 6003-13
2. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144, 271-8
3. Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143-144, 247-53
4. Structural basis and mechanism of enoyl reductase inhibition by triclosan. J. Mol. Biol. 290, 859-65
5. Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI). J. Med. Chem. 45, 3246-56
6. Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK. J. Med. Chem. 46, 1627-35
7. Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Sci. 8, 2529-32
8. Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan. Biochemistry 38, 12514-25
9. Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279, 98-102
10. Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase. Structure 3, 927-38