1.1.1.50 3-acetylpyridine adenine dinucleotide i.e. APAD+, 42% of the activity with NAD+ when cholic acid is utilized as substrate 656300 1.1.1.50 additional information cofactor specificity with different substrates 656300 1.1.1.50 additional information cytosolic and microsomal enzymes have different cofactor preferences: cytosolic enzymes prefer NADP+/NADPH, microsomal prefer NAD+/NADH 389541 1.1.1.50 additional information kinetic model involving cofactor-enzyme complex formation kinetics 654186 1.1.1.50 additional information see also EC 1.1.1.213 for enzymes catalyzing the same reaction but with A-specificity concerning the cofactor, all enzymes without information of stereospecificity for cofactors are included in EC 1.1.1.50, but some of those may in fact belong to EC 1.1.1.213 389522 1.1.1.50 NAD(P)+ - 655790, 689169, 696786 1.1.1.50 NAD(P)H - 655790, 689169 1.1.1.50 NAD(P)H 1000fold lower activity with NADH compared to NADPH 673349 1.1.1.50 NAD(P)H cofactor binding structure, overview 674674 1.1.1.50 NAD+ - 347986, 389560, 654186, 656200, 656838, 669389, 674981, 687642, 696459, 740802, 741274, 741361 1.1.1.50 NAD+ best cofactor, preferably utilized with substrate cholic acid 656300 1.1.1.50 NAD+ oxidation utilizing NAD+ as a cofactor is the preferred reaction in vitro 655348 1.1.1.50 NAD+ preference for 389541 1.1.1.50 NAD+ preferred by AKR1C17, dependent on, residues Gln270 and Glu276 are important for cofactor specificity, overview 684676 1.1.1.50 NAD+ specific, enzyme does not use NADP+ 389548 1.1.1.50 NADH - 389546, 654186, 655348, 656838, 669389, 671112, 674981, 684676, 687642, 711310, 740802, 741274, 741361 1.1.1.50 NADH cytosolic 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity 389560 1.1.1.50 NADH NADH association to enzyme involves a bimolecular binding step and isomerization. The binding of NADH into a hydrophobic pocket in the active site restricts its motion and shields the fluorescence quenching from solvent 696459 1.1.1.50 NADH plasma membrane NADH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity 389557, 389558, 389559, 389561 1.1.1.50 NADH preference for 389541 1.1.1.50 NADP+ - 347986, 389547, 389549, 655348, 656200, 656642, 656838, 672088, 740017, 741098 1.1.1.50 NADP+ binding and release mechanism 655214 1.1.1.50 NADP+ binding structure and mechanism, overview 738928 1.1.1.50 NADP+ binding to isozyme AKR1C2, mechanism and structure 656651 1.1.1.50 NADP+ loose association of the NADP(H) is followed by two conformational changes, which increases cofactor affinity by 86fold 687635 1.1.1.50 NADP+ preferred by AKR1C9, dependent on, residues Gln270 and Glu276 are important for cofactor specificity, overview 684676 1.1.1.50 NADPH - 389547, 389549, 389562, 654626, 654924, 655215, 655348, 656642, 656648, 656838, 675595, 676812, 684676, 685529, 738928, 740017, 741098 1.1.1.50 NADPH binding and release mechanism 655214 1.1.1.50 NADPH comparison of NADPH with deuterium-substituted NADPD, overview 672088 1.1.1.50 NADPH cytosolic NADPH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity 389557, 389558, 389559, 389561 1.1.1.50 NADPH dependent on 656200 1.1.1.50 NADPH loose association of the NADP(H) is followed by two conformational changes, which increases cofactor affinity by 86fold 687635 1.1.1.50 NADPH NADPH-linked microsomal 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase shows very low activity only with NADPH 389560 1.1.1.50 NADPH preference for 389544, 389545, 389556, 587068 1.1.1.50 nicotinamide hypoxanthine dinucleotide i.e. deamino-NAD+, 36% of the activity with NAD+ when cholic acid is utilized as substrate 656300 1.1.1.50 thio-NAD+ - 654186 1.1.1.50 thio-NAD+ 47% of the activity with NAD+ when cholic acid is utilized as substrate, preferably utilized with substrate fusidic acid 656300