Common themes in redox chemistry emerge from the X-ray structure of oilseed rape ( Brassica napus) enoyl acyl carrier protein reductase

Background: Enoyl acyl carrier protein reductase (ENR) catalyzes the NAD(P)H-dependent reduction of trans- Δ2-enoyl acyl carrier protein, an essential step in de novo fatty acid biosynthesis. Plants contain both NADH-dependent and separate NADPH-dependent ENR enzymes which form part of the dissociable type II fatty acid synthetase. Highly elevated levels of the NADH-dependent enzyme are found during lipid deposition in maturing seeds of oilseed rape ( Brassica napus). Results The crystal structure of an ENR–NAD binary complex has been determined at 1.9 å resolution and consists of a homotetramer in which each subunit forms a single domain comprising a seven-stranded parallel β sheet flanked by seven α helices. The subunit has a topology highly reminiscent of a dinucleotide-binding fold. The active site has been located by difference Fourier analysis of data from crystals equilibrated in NADH. Conclusion The structure of ENR shows a striking similarity with the epimerases and short-chain alcohol dehydrogenases, in particular, 3 α,20 β-hydroxysteroid dehydrogenase (HSD). The similarity with HSD extends to the conservation of a catalytically important lysine that stabilizes the transition state and to the use of a tyrosine as a base — with subtle modifications arising from differing requirements of the reduction chemistry.