Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli.
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.
Donahue
J L
JL
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061, USA.
Bownas
J L
JL
Niehaus
W G
WG
Larson
T J
TJ
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology; D002384:Catalysis; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D006597:Fructose-Bisphosphatase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology; D015870:Gene Expression; D005994:Glycerophosphates / Q000378:metabolism*; D008970:Molecular Weight; D018085:Regulon; D013379:Substrate Specificity
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D005994:Glycerophosphates; C077563:GlpX protein, E coli; C029620:alpha-glycerophosphoric acid; D006597:Fructose-Bisphosphatase