STUDIES ON THE BIOSYNTHESIS OF THE α-GLUCOSIDASE INHIBITOR ACARBOSE: VALIENAMINE, A m-C7N UNIT NOT DERIVED FROM THE SHIKIMATE PATHWAY

URSULA DEGWERT; ROSEMARIE VAN HÜLST; HERMANN PAPE; RICHARD E. HERROLD; JOHN M. BEALE; PAUL J. KELLER; JONATHAN P. LEE; HEINZ G. FLOSS

doi:10.7164/antibiotics.40.855

STUDIES ON THE BIOSYNTHESIS OF THE α-GLUCOSIDASE INHIBITOR ACARBOSE: VALIENAMINE, A m-C₇N UNIT NOT DERIVED FROM THE SHIKIMATE PATHWAY

URSULA DEGWERT, ROSEMARIE VAN HÜLST, HERMANN PAPE, RICHARD E. HERROLD, JOHN M. BEALE, PAUL J. KELLER, JONATHAN P. LEE, HEINZ G. FLOSS

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JOURNAL FREE ACCESS

1987 Volume 40 Issue 6 Pages 855-861

DOI https://doi.org/10.7164/antibiotics.40.855

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Abstract

Feeding experiments with Actinoplanes sp. SN223/29 showed that 3-amino-5-hydroxy[7-]SP13C]benzoic acid is not incorporated into acarbose (I). The valienamine moiety of I is thus not derived in the same way, from the shikimate pathway, as the m-C₇N units in the ansamycin, mitomycin and ansamitocin antibiotics. Feeding experiments with [U-¹³C₃]glycerol followed by analysis of I by multiple quantum NMR spectroscopy support this conclusion and point to formation of the valienamine moiety by cyclization of a heptulose phosphate which arises from a triose phosphate via successive transfer of two 2-carbon fragments by transketolase, as proposed by PAPE and co-workers.

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