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
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Bacterial Proteins / physiology
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Catalysis
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Cloning, Molecular
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins*
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Fructose-Bisphosphatase / genetics
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Fructose-Bisphosphatase / isolation & purification
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Fructose-Bisphosphatase / metabolism*
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Fructose-Bisphosphatase / physiology
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Gene Expression
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Glycerophosphates / metabolism*
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Molecular Weight
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Regulon*
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Substrate Specificity
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Glycerophosphates
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GlpX protein, E coli
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alpha-glycerophosphoric acid
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Fructose-Bisphosphatase