New enzymatic assay for the AKR1C enzymes

Chemico-Biological Interactions

Volumn 202, Issue 1-3, 2013, Pages 204-209

  Beranič, Nataša ^a   Štefane, Bogdan ^a,b   Brus, Boris ^a   Gobec, Stanislav ^a   Rižner, Tea Lanišnik ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

^b EN FIST CENTRE OF EXCELLENCE   (Slovenia)

Author keywords

AKR1C isoforms; Artificial substrates; Cyclopentane derivatives; Enzymatic assay

Indexed keywords

2 (4 CHLOROBENZYLIDENE)CYCLOPENTANOL; 2 (4 CHLOROBENZYLIDENE)CYCLOPENTANONE; ALDO KETO REDUCTASE 1C1; ALDO KETO REDUCTASE 1C2; ALDO KETO REDUCTASE 1C3; ENZYME INHIBITOR; MEDROXYPROGESTERONE ACETATE; OXIDOREDUCTASE; UNCLASSIFIED DRUG; URSODEOXYCHOLIC ACID;

CATALYSIS; CHEMICAL ANALYSIS; CHEMICAL STRUCTURE; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME PURIFICATION; MOLECULAR DOCKING; NONHUMAN; OXIDATION; PROTEIN EXPRESSION; SIMULATION; SPECTROPHOTOMETRY;

20-HYDROXYSTEROID DEHYDROGENASES; 3-HYDROXYSTEROID DEHYDROGENASES; ALCOHOL OXIDOREDUCTASES; CATALYSIS; CYCLOPENTANES; ENZYME ASSAYS; ENZYME INHIBITORS; HUMANS; HYDROXYPROSTAGLANDIN DEHYDROGENASES; KINETICS; MEDROXYPROGESTERONE ACETATE; NAD; NADP; OXIDATION-REDUCTION; URSODEOXYCHOLIC ACID;

EID: 84875226116     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2012.12.003     Document Type: Conference Paper

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