carbonyl reductase (NADPH)

This is an abbreviated version, for detailed information about carbonyl reductase (NADPH), go to the full flat file.




15-hydroxyprostaglandin dehydrogenase [NADP+], 2,5-diketo-D-gluconic acid reductase, Adipocyte P27 protein, aldehyde reductase 1, aldehyde reductase I, aldo-keto reductase, ALR3, AP27, carbonyl reductase, carbonyl reductase (NADPH), carbonyl reductase 1, carbonyl reductase 3, carbonyl reductase S1, CBR, CBR 1, CBR 3, CBR1, CBR3, CHCR, CHCR1, CHCR2, CHCR3, CR, CSCR1, Gox0644, Gox1615, hCBR1, ketoreductase, KLCR1, KR, LCR, LOC415661, LOC610164, microsomal carbonyl reductase, More, NADP+-dependent ADH, NADPH-carbonyl reductase, NADPH-dependent carbonyl reductase, NADPH-dependent carbonyl reductase S1, NCCR, nonspecific NADPH-dependent carbonyl reductase, peroxisomal-type carbonyl reductase, PHCR, prostaglandin 9-ketoreductase, Prostaglandin-E2 9-reductase, PTCR, R-specific carbonyl reductase, reductase S1, reductase, carbonyl, RLCR, SCR, SDR21C1, secondary-alcohol: NADP+-oxidoreductase, short-chain (S)-1-phenyl-1,2-ethanediol dehydrogenase, short-chain carbonyl reductase, sniffer, SSCR, tetrameric carbonyl reductase, Tm1743, Tm_1743, xenobiotic carbonyl reductase, xenobiotic ketone reductase, YGL039w1, YGL039w2, YtbE


     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
       carbonyl reductase (NADPH)


Crystallization on EC - carbonyl reductase (NADPH)

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three-dimensional strcuture determined by molecular replacement at a resolution of 2.09 A, in the presence of NADPH. Extensive formation of the intrasubunit ion pair networks, and the presence of the strong intersubunit interaction, is likely responsible for thermostability
purified detagged recombinant enzyme, sitting-drop vapour-diffusion method, protein solution is supplemented with 5 mM beta-NADPH, crystallization from 31% v/v PEG 400, 0.2 M Li2SO4, 0.08 M sodium potassium tartrate tetrahydrate, 0.1 M sodium cacodylate, pH 6.5, at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.90 A resolution
apo-enzyme, diffraction to 2.7 A. Enzyme forms a homotetramer with broken 2-2-2 symmetry. In the apo-form, the entrance of the NADPH pocket is blocked by a surface loop
by the hanging-drop vapor diffusion method, to 2.7 A resolution, crystal form belongs to space group P212121 with cell dimensions of a=104.7 A, b=142.8 A, and c=151.8 A. It forms a homotetramer with a broken 2-2-2 symmetry. SCR contains an extended N-terminal peptide (i.e., residues 1-25) and a short helix (residues 26-30) projecting out from the core domain that may stabilize the oligomer. In the apo-SCR structure, the entrance of the NADPH pocket is blocked by a surface loop
homology modeling of native enzyme, enzyme lacking the extra loop domain, and exchange of the extra loop domain for the short extra loop of 3alpha/20beta-hydroxysteroid dehydrogenase
purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml water with 0.003 ml protein solution and 0.003 ml reservoir solution giving 18% w/v PEG 4000, 0.15 M sodium acetate, 75 mM Tris, pH 8.5, severeal days at 4°C, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular modeling
molecular replacement, to 1.98 A resolution in presence of NADPH and ethylene glycol
computational docking experiments for four inhibitors. For flavonoid inhibitors, the flavonoid skeleton is the binding part of the molecule and sugar moieties are pointing outward, giving rise to a stabilizing effect
in complex with glutathione, in the absence of its substrates or inhibitors. The glutathione molecule contributes to the substrate selectivity and protects the catalytic center of hCBR1 through a switch-like mechanism. Glutathione directly binds with hCBR1 when there’s no substrate
recombinant protein from Escherichia coli
computational model of docking of 4¢-methoxyacetophenone to the Q245H mutant
purified recombinant free wild-type or selenomethionine-labeled enzyme and in complex with NADPH, vapour disffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, against a reservoir solution containing 32% w/v PEG 2000 monomethyl ether, 100 mM ammonium sulfate, and 0.2 M sodium acetate, pH 5.0, with or without 4 mM NADPH, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, structure modeling
5 mg/ml recombinant enzyme in 25 mM phosphate buffer, pH 8.0, with 10% glycerol, and 5 mM NADP+, hanging drop vapour diffusion method, against well solution containing 4.0-4.4 M sodium formate and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.5 A resolution
C-terminal peroxisomal targeting sequence 1 of each subunit is involved in intersubunit interactions and buried in the interior of the tetrameric enzyme
crystallization to crystal forms I and II in the presence of NADPH. Form I crystals belong to the tetragonal space group P42, and diffract to 1.5 A resolution. Form II crystals belong to the tetragonal space group P41212, and diffract to 2.2 A resolution; purified and dialyzed recombinant enzyme complexed with cofactor, 3 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM NADPH, hanging drop vapour diffusion method, 0.002 ml of protein and crystallization solutions are mixed at 20°C, and equilibrated against 0.5 ml reservoir solution, which contains 2.2 M sodium citrate and 20%(v/v) glycerol in 100 mM HEPES buffer, pH 7.5 or 1.4 M ammonium sulfate and 20%(v/v) glycerol in 100 mM MES buffer pH 6.0, resulting in two different tetragonal crystal forms, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.2 A resolution
in complex with cofactor NADP+ and with NADP+ and substrate ethyl 2-oxo-4-phenylbutyrate, to 1.7 and 2.0 A resolution, respectively. Both crystals belong to space group P3121, with similar unit-cell parameters