title: Kinetic properties of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli 080.
abstract: Results on the kinetics of 7 alpha-hydroxysteroid dehydrogenase 7 alpha-HSDH showed that this enzyme could oxidize all bile acids having an -OH group at the C-7 position. Lineweaver-Burk plots showed Michaelis constant (Km) values of 0.83 and 0.12 mM for cholic acid and chenodeoxycholic acid, respectively. The effect of enzyme concentration on the reaction velocity showed a constant increase in the enzyme activity with increase in enzyme-protein concentration. 7 alpha-HSDH was activated by Na+, K+, Ca2+, and Mn2+ ions and by reducing agents having a thiol group (dithiothreitol, 2-mercaptoethanol). Co2+, Hg2+, Fe3+, Mg2+, Zn2+, Ba2+, and Cu2+ ions, chelating agents (potassium oxalate, heparin, EDTA) oxidizing agents (sodium perchlorate, sodium periodate, sodium persulphate), and detergents (Tween 20, Tween 40, Tween 80, Triton X-100, sodium lauryl sulphate) were inhibitory to 7 alpha-HSDH activity.
authors.affiliation: Department of Microbiology, Panjab University, Chandigarh, India.
authors.forename: V
authors.initials: V
authors.lastname: Prabha
authors.forename: M
authors.initials: M
authors.lastname: Gupta
authors.forename: K G
authors.initials: KG
authors.lastname: Gupta
mesh_terms: D001647:Bile Acids and Salts / Q000378:metabolism*; D002614:Chelating Agents / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D006913:Hydroxysteroid Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D001647:Bile Acids and Salts; D002614:Chelating Agents; D003902:Detergents; D008670:Metals; D006913:Hydroxysteroid Dehydrogenases; C025376:7 alpha-hydroxysteroid dehydrogenase