Identification of a 1-epi-valienol 7-kinase activity in the producer of acarbose, Actinoplanes sp. SE50/110.
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.
Zhang
Chang-Sheng
CS
Institute of Chemical Microbiology, Bergische University, Gauss-Str 20, D-42097 Wuppertal, Germany.
Podeschwa
Michael
M
Block
Oliver
O
Altenbach
Hans-Josef
HJ
Piepersberg
Wolfgang
W
Wehmeier
Udo F
UF
D020909:Acarbose / Q000737:chemistry / Q000378:metabolism*; D000192:Actinomycetales / Q000378:metabolism*; D002240:Carbohydrate Sequence; D002855:Chromatography, Thin Layer; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010770:Phosphotransferases / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization
D010770:Phosphotransferases; D020909:Acarbose