NAD+ is situated in a cleft of PnpE. The cofactor binding site is composed of two pockets. The adenosine and the first ribose group of NAD bind in one pocket and the nicotinamide ring in the other. Six amino acids, C281, E247, Q210, W148, I146 and K172, interact with the cofactor
the pnpE-encoded enzyme gamma-hydroxymuconic semialdehyde dehydrogenase catalyzes the reduction of 4-hydroxymuconic semialdehyde to maleylacetate in Pseudomonas sp. strain WBC-3, playing a key role in the catabolism of toxic para-nitrophenol to Krebs cycle intermediates
highly conserved residues C281 and E247 are identified to be critical for its catalytic activity, and flexible docking studies of the enzyme-substrate system predict the interactions between PnpE and its substrate 4-hydroxymuconic semialdehyde, flexible docking of substrate to PnpE, molecular docking analysis, overview
the monomer of PnpE has the typical structural organization betaalphabeta of the ALDH family, with 17 beta-strands and 14 alpha-helices, the secondary structures belong to three domains: a substrate binding domain, a cofactor binding domain, and an oligomerization domain mediating protein dimerization. The substrate binding domain consists of a central six-stranded beta-sheet and six alpha-helices, while the cofactor binding domain contains a nine-stranded beta-sheet and seven alpha-helices, structure, overview
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purified recombinant enzyme PnpE in apo-form or in complex with NAD+, sitting drop vapor diffusion technique, 10 mg/ml apo-enzyme from 20% w/v PEG 3350, and 0.2 M KNO3 at 20°C, 10 mg/ml NAD+-complexed enzyme from 0.1 M bicine, pH 8.5, 20% PEG 10000, and 1 mM NAD+, X-ray diffraction structure determination and analysis at 2.7-3.1 A resolution, molecular replacement method using bovine mitochondrial aldehyde dehydrogenase, PDB ID 1A4Z, as the search model