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Identification of a 1‐<i>epi</i>‐valienol 7‐kinase activity in the producer of acarbose, <i>Actinoplanes</i> sp. SE50/110
19
Citations
9
References
2003
Year
Acb GeneGlycobiologyKinase ReactionBiosynthesisNew Kinase ActivityReceptor Tyrosine KinaseCell SignalingProtein FunctionBiochemistryMechanism Of ActionBiomolecular InteractionCell BiologyProtein PhosphorylationProtein BiosynthesisSignal TransductionNatural SciencesCellular BiochemistrySystems BiologyMedicine
In the biosynthesis of the C7-cyclitol moiety, valienol, of the alpha-glucosidase inhibitor acarbose in Actinoplanes sp. SE50/110 various cyclitol phosphates, such as 1-epi-valienol-7-phosphate, are postulated precursors. In the cell extracts of Actinoplanes SE50/110 we found a new kinase activity which specifically phosphorylates 1-epi-valienol; other C7-cyclitol analogs were only weakly or not phosphorylated. The purified product of the kinase reaction turned out to be 1-epi-valienol-7-phosphate in analyses by nuclear magnetic resonance spectroscopy. The enzyme seems not to be encoded by an acb gene and, therefore, plays a role in a salvage pathway rather than directly in the de novo biosynthesis of acarbose.
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