Abstract
A Pasteurella multocida N-acetylglucosamine 1-phosphate uridylyltransferase (PmGlmU) was cloned and used efficiently with an N-acetylhexosamine 1-kinase (NahK_ATCC55813) and an inorganic pyrophosphatase (PmPpA) for one-pot three-enzyme synthesis of UDP-GlcNAc derivatives with or without further chemical diversification.
This journal is © The Royal Society of Chemistry 2011
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Acetylglucosamine / chemical synthesis
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Acetylglucosamine / chemistry*
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Bacterial Proteins / metabolism*
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Bifidobacterium / enzymology
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Inorganic Pyrophosphatase / metabolism*
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Nucleotidyltransferases / metabolism*
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Pasteurella multocida / enzymology
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Uridine Diphosphate N-Acetylglucosamine / chemical synthesis*
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Uridine Diphosphate N-Acetylglucosamine / chemistry
Substances
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Bacterial Proteins
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Uridine Diphosphate N-Acetylglucosamine
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Nucleotidyltransferases
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UDPacetylglucosamine pyrophosphorylase
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Inorganic Pyrophosphatase
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Acetylglucosamine