Studies on the substrate specificity of a GDP-mannose pyrophosphorylase from <i>Salmonella enterica</i>

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<jats:p>A series of methoxy and deoxy derivatives of mannopyranose-1-phosphate (Man<jats:italic>p</jats:italic>-1P) were chemically synthesized, and their ability to be converted into the corresponding guanosine diphosphate mannopyranose (GDP-Man<jats:italic>p</jats:italic>) analogues by a pyrophosphorylase (GDP-ManPP) from <jats:italic>Salmonella enterica</jats:italic> was studied. Evaluation of methoxy analogues demonstrated that GDP-ManPP is intolerant of bulky substituents at the C-2, C-3, and C-4 positions, in turn suggesting that these positions are buried inside the enzyme active site. Additionally, both the 6-methoxy and 6-deoxy Man<jats:italic>p</jats:italic>-1P derivatives are good or moderate substrates for GDP-ManPP, thus indicating that the C-6 hydroxy group of the Man<jats:italic>p</jats:italic>-1P substrate is not required for binding to the enzyme. When taken into consideration with other previously published work, it appears that this enzyme has potential utility for the chemoenzymatic synthesis of GDP-Man<jats:italic>p</jats:italic> analogues, which are useful probes for studying enzymes that employ this sugar nucleotide as a substrate.</jats:p>

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