Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+ - Test2 - elhamkhani - TriplyDB

Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

http://www.wikidata.org/entity/Q27733250

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Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones Why boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiation Insights in 17beta-HSD1 enzyme kinetics and ligand binding by dynamic motion investigation Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases Crystal Structure of Human Liver 4-3-Ketosteroid 5 -Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis Structure and catalytic mechanism of human steroid 5β-reductase (AKR1D1)Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase fromStreptococcus suis: Crystal structures of the substrate-free and quaternary complex enzymes Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes during NADPH Binding Functional studies of aldo-keto reductases in Saccharomyces cerevisiae Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins Regulation of ecdysteroid signalling: molecular cloning, characterization and expression of 3-dehydroecdysone 3 alpha-reductase, a novel eukaryotic member of the short-chain dehydrogenases/reductases superfamily from the cotton leafworm, Spodoptera Comparative anatomy of the aldo-keto reductase superfamily Alteration of a single amino acid changes the substrate specificity of dihydroflavonol 4-reductase.Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms.Human hydroxysteroid dehydrogenases and pre-receptor regulation: insights into inhibitor design and evaluation.The aldo-keto reductases (AKRs): Overview.Aldo-keto reductase (AKR) superfamily: genomics and annotation.Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2α synthase, AKR1B3.Aldo-keto reductases and formation of polycyclic aromatic hydrocarbon o-quinones.Human carbonyl reduction pathways and a strategy for their study in vitro.Topography and function of androgen-metabolizing enzymes in the central nervous system.Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens.Current physico-biochemistry in steroid research and status of structural biology for steroid-converting enzymes.Human aldo-keto reductases: structure, substrate specificity and roles in tumorigenesis.Identification of amino acid residues responsible for differences in substrate specificity and inhibitor sensitivity between two human liver dihydrodiol dehydrogenase isoenzymes by site-directed mutagenesis Aldo-keto reductases in which the conserved catalytic histidine is substituted Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an "induced-fit" mechanism and a conserved basic motif involved in the binding of androgen.Transient-phase kinetic studies on the nucleotide binding to 3alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831 using fluorescence stopped-flow procedures.The aldo-keto reductase superfamily and its role in drug metabolism and detoxification

P2860

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P2860

Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

http://www.wikidata.org/entity/Q27733250

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1996 nî lūn-bûn

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP + †

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+

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