Glucose-6-phosphate dehydrogenase from Escherichia coli and from a "high-level" mutant.
Glucose-6-phosphate dehydrogenase has been purified to near homogeneity from wild-type Escherichia coli K-12 and from a mutant previously found to contain substantially more of the enzyme. The two enzymes are the same in all characteristics studied thus far: specific activity, kinetics, specificity, and subunit size.
D000255:Adenosine Triphosphate; D000538:Aluminum Silicates; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D004589:Electrophoresis, Disc; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D005827:Genetics, Microbial; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D006882:Hydroxyapatites; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium; D009154:Mutation; D009243:NAD; D009249:NADP; D012967:Sodium Dodecyl Sulfate
D000538:Aluminum Silicates; D006882:Hydroxyapatites; D046911:Macromolecular Substances; D009243:NAD; D012967:Sodium Dodecyl Sulfate; D009249:NADP; D000255:Adenosine Triphosphate; D005954:Glucosephosphate Dehydrogenase; D008274:Magnesium