Abstract
Escherichia coli cytosolic glycerophosphodiester phosphodiesterase, UgpQ, functions in the absence of other proteins encoded by the ugp operon and requires Mg2+, Mn2+, or Co2+, in contrast to Ca2+-dependent periplasmic glycerophosphodiester phosphodiesterase, GlpQ. UgpQ has broad substrate specificity toward various glycerophosphodiesters, producing sn-glycerol-3-phosphate and the corresponding alcohols. UgpQ accumulates under conditions of phosphate starvation, suggesting that it allows the utilization of glycerophosphodiesters as a source of phosphate. These results clarify how E. coli utilizes glycerophosphodiesters using two homologous enzymes, UgpQ and GlpQ.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cobalt / metabolism
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Cytosol / metabolism
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli / growth & development
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Gene Expression Regulation, Bacterial
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Immunoblotting
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Magnesium / metabolism
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Manganese / metabolism
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Metals / metabolism*
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Phosphates / metabolism
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Phosphoric Diester Hydrolases / genetics
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Phosphoric Diester Hydrolases / metabolism*
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Protons
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Metals
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Phosphates
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Protons
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Recombinant Proteins
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Cobalt
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Manganese
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Phosphoric Diester Hydrolases
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glpQ protein, Bacteria
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glycerophosphodiester phosphodiesterase
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Magnesium