Jb. Rafferty et al., COMMON THEMES IN REDOX CHEMISTRY EMERGE FROM THE X-RAY STRUCTURE OF OILSEED RAPE (BRASSICA-NAPUS) ENOYL ACYL CARRIER PROTEIN REDUCTASE, Structure, 3(9), 1995, pp. 927-938
Background: Enoyl acyl carrier protein reductase (ENR) catalyzes the N
AD(P)H-dependent reduction of trans-Delta 2-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 fo
rm part of the dissociable type II fatty acid synthetase. Highly eleva
ted levels of the NADH-dependent enzyme are found during lipid deposit
ion in maturing seeds of oilseed rape (Brassica napus). Results: The c
rystal structure of an ENR-NAD binary complex has been determined at 1
.9 Angstrom resolution and consists of a homotetramer in which each su
bunit forms a single domain comprising a seven-stranded parallel beta
sheet flanked by seven alpha helices. The subunit has a topology highl
y reminiscent of a dinucleotide-binding fold. The active site has been
located by difference Fourier analysis of data from crystals equilibr
ated in NADH. Conclusions: The structure of ENR shows a striking simil
arity with the epimerases and short-chain alcohol dehydrogenases, in p
articular, 3 alpha,20 beta-hydroxysteroid dehydrogenase (HSD). The sim
ilarity with HSD extends to the conservation of a catalytically import
ant lysine that stabilizes the transition state and to the use of a ty
rosine as a base - with subtle modifications arising from differing re
quirements of the reduction chemistry.