Purification and Characterization of glpX -Encoded Fructose 1,6-Bisphosphatase, a New Enzyme of the Glycerol 3-Phosphate Regulon of Escherichia coli

Author:

Donahue Janet L.1,Bownas Jennifer L.1,Niehaus Walter G.1,Larson Timothy J.1

Affiliation:

1. Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061

Abstract

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 μM for fructose 1,6-bisphosphate. The enzyme was inhibited by ADP and phosphate and activated by phosphoenolpyruvate.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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