PMID:10986273
| Citation |
Donahue, JL, Bownas, JL, Niehaus, WG and Larson, TJ (2000) Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J. Bacteriol. 182:5624-7 |
|---|---|
| Abstract |
In Escherichia coli, gene products of the glp regulon mediate utilization of glycerol and sn-glycerol 3-phosphate. The glpFKX operon encodes glycerol diffusion facilitator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the previously described fbp-encoded enzyme. The purified enzyme was dimeric, dependent on Mn(2+) for activity, and exhibited an apparent K(m) of 35 microM for fructose 1,6-bisphosphate. The enzyme was inhibited by ADP and phosphate and activated by phosphoenolpyruvate. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Catalysis; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Fructose-Bisphosphatase/genetics; Fructose-Bisphosphatase/isolation & purification; Fructose-Bisphosphatase/metabolism; Fructose-Bisphosphatase/physiology; Gene Expression; Glycerophosphates/metabolism; Molecular Weight; Regulon; Substrate Specificity |
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