Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by x-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 A resolution. The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an alpha/beta-barrel with the active site located at the carboxy terminus of the strands of the barrel. Unlike aldose reductase, the N epsilon 2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH.
The effect of several metal ions on the production of diphtheria toxin was tested. By using the gel immunodiffusion system for detecting toxin, a wide range of metal ion concentrations was conveniently surveyed. Five divalent cations, Fe2+, Cu2+, Co2+, Ni2+, and Mn2+ inhibited toxin production within a range of concentrations that did not inhibit growth of the producing strain. Growth and toxin production were inhibited at identical concentrations by both Cd2+ and Zn2+, whereas A13+ and Sr2`affected neither growth nor toxin production over the range of concentrations tested. The data showed that Fe2+ was the most
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