Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
about
sameAs
Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retinaHuman 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 hormonesWhy boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiationInsights in 17beta-HSD1 enzyme kinetics and ligand binding by dynamic motion investigationStructure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolutionStructure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductasesThe crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductasesCrystal Structure of Human Liver 4-3-Ketosteroid 5 -Reductase (AKR1D1) and Implications for Substrate Binding and CatalysisStructure 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 enzymesCrystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes during NADPH BindingFunctional studies of aldo-keto reductases in Saccharomyces cerevisiaeConversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestinsRegulation 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, SpodopteraComparative anatomy of the aldo-keto reductase superfamilyAlteration 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 metabolismHuman 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 mutagenesisAldo-keto reductases in which the conserved catalytic histidine is substitutedComparison 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
Q24306659-3182EFD5-7833-44CF-B691-C0006CAE808EQ24532164-6735A5C2-B1C4-45B9-B4CC-3D119A6B142EQ24618043-B72093AC-6215-465A-820C-4D0F47266EF4Q27322084-247E2B19-DA15-4C65-8FED-A00E8A092BE3Q27634265-ECA5EB58-F428-498E-ADA0-81362AA63550Q27641163-BD2591C0-B67E-4E53-B8B3-0D289AFFD384Q27649122-EAE2EAF2-83A9-4B3C-B6E4-C31EC27FEEE9Q27650311-763AF135-717C-46AB-8DC4-E89F76E49A99Q27652485-36C4070C-5D33-4EB1-AAB5-F98B4144E5D2Q27653597-9E77D220-49DA-4D44-B8A3-7648C23A0362Q27677286-4A289B68-A75A-4F34-A00E-671C1AD58581Q27938824-0B2424A3-679B-4DF6-8312-6820143099B2Q28343598-61458FD7-A8BB-4570-924F-BD4085BBE23BQ28344368-82DA3DCC-6457-4C37-9E2A-D32542E1CA2CQ30043211-4E268612-40D6-4433-8D63-0848C91B619FQ32029014-8896F281-1398-4706-BDCE-37314B24B408Q34382405-5CB40BE8-FC88-48BC-AF3C-A57019951FB5Q34632786-D1948C76-DE8E-4988-81D7-68E7DD73EFF0Q35013689-AF0C04BD-1507-4D93-BEAD-7456C12F35CFQ35305934-90C0C48F-5E20-4838-AB74-719BA47B39C5Q35503117-66EC4AEA-1ADC-49F9-A31F-1C4D780C48DFQ35596643-10781A5F-1865-4971-B5F3-88E8727A1240Q35707890-1CDB6645-4659-43E9-94D3-B81879BFA32DQ35828036-C3D52C58-C4D4-45D6-9C3D-386A810542FBQ36081807-8CF304B3-A108-448C-875B-2F4B9EC21AD7Q37002896-1C1D2127-B280-49AD-8BE3-1D03D2034953Q37612901-08E6BD49-90E8-458F-A69C-6241E5095C78Q38472538-D4D008BD-07EA-48FA-BC82-D0C087C75859Q42132854-9EB8A32E-18AF-4D5E-AA7C-A25016E71005Q42582810-0F8A954F-D1E6-4043-8C45-47DFA5F3CF9FQ43057981-387BB6A2-35E1-44C2-92BD-2CE11D52C045Q44850891-97FBC98B-03AC-42E2-AB5F-3B9328A2D7B1Q56760512-89B99C1B-CD55-46DD-856E-95A2D8916E85
P2860
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@ast
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@en
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@nl
type
label
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@ast
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@en
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@nl
altLabel
Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP + †
@en
prefLabel
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@ast
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@en
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@nl
P2093
P356
P1433
P1476
Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+
@en
Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP + †
@en
P2093
B P Schlegel
Brian P. Schlegel
Joseph M. Jez
M J Bennett
Melanie J. Bennett
Mitchell Lewis
T M Penning
Trevor M. Penning
P304
P356
10.1021/BI9604688
P407
P577
1996-01-01T00:00:00Z
1996-08-20T00:00:00Z