Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli

J Bacteriol. 2000 Oct;182(19):5624-7. doi: 10.1128/JB.182.19.5624-5627.2000.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • 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

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Glycerophosphates
  • GlpX protein, E coli
  • alpha-glycerophosphoric acid
  • Fructose-Bisphosphatase