Abstract
The eryA gene of the bacterial pathogen Brucella abortus has been functionally expressed in Escherichia coli. The resultant EryA was shown to catalyze the ATP-dependent conversion of erythritol to L-erythritol-4-phosphate (L-E4P). The steady state kinetic parameters of this reaction were determined and the enzyme was used to prepare L-E4P which was shown to be a weak inhibitor of 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase (YgbP).
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Brucella abortus / enzymology*
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Cloning, Molecular
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Erythritol / analogs & derivatives*
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Erythritol / biosynthesis*
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Erythritol / metabolism
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Erythritol / pharmacology
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Kinetics
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Nucleotidyltransferases / antagonists & inhibitors
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Phosphotransferases (Alcohol Group Acceptor) / genetics
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Phosphotransferases (Alcohol Group Acceptor) / metabolism*
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Sugar Phosphates / biosynthesis*
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Sugar Phosphates / pharmacology
Substances
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Sugar Phosphates
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erythritol 4-phosphate
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Adenosine Triphosphate
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Phosphotransferases (Alcohol Group Acceptor)
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erythritol kinase
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2-C-methyl erythritol 4-phosphate cytidylyltransferase
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Nucleotidyltransferases
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Erythritol