6-phosphogluconolactonase. Purification, properties and activities in various tissues.
6-Phosphogluconolactonase was purified to apparent homogeneity in a four-step procedure from bovine erythrocytes. The extent of purification and the kinetic properties of the enzyme were evaluated with an optical test that was based on the hydrolysis of synthetic 6-phosphogluconolactone. The active enzyme from bovine erythrocytes is a monomer with an approximate molecular weight of 30000. It exhibits Michaelis-Menten kinetics and cofactors are not required for activity. The enzyme was found in a number of tissues. Its activity, when compared to the activity of the glycolytic enzymes, illustrates the importance of glucose oxidation via the pentose phosphate pathway relative to glycolysis.
D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000097:blood / Q000302:isolation & purification*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004586:Electrophoresis / Q000379:methods; D004912:Erythrocytes / Q000201:enzymology; D006019:Glycolysis; D006801:Humans; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D009206:Myocardium / Q000201:enzymology; D051381:Rats
D002265:Carboxylic Ester Hydrolases; C022363:6-phosphogluconolactonase