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- Molecular Detection of [alpha]-Glucosidase Inhibitor-producing Actinomycetes
- Chang-Gu Hyun , Seung-Young Kim , Jin-Haeng Hur , Myung-Ji Seo , Joo-Won Suh , Soon-Ok Kim
- J. Microbiol. 2005;43(3):313-318.
- DOI: https://doi.org/2207 [pii]
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Abstract
- In this study, we demonstrate the use of a PCR-based method for the detection of the specific genes involved in natural-product biosynthesis. This method was applied, using specifically designed PCR primers, to the amplification of a gene segment encoding for sedo-heptulose 7-phosphate cyclase, which appears to be involved in the biosynthetic pathways of C_7N aminoacyclitol or its keto analogue-containing metabolites, in a variety of actinomycetes species. The sequences of DNA fragments (about 540 bp) obtained from three out of 39 actinomycete strains exhibited a high degree of homology with the sedo-heptulose 7-phosphate cyclase gene, which has been implicated in acarbose biosynthesis. The selective cultivation conditions of this experiment induced the expression of these loci, indicating that the range of C_7N aminoacyclitol or its keto analogue-group natural products might be far greater than was previously imagined. Considering that a total of approximately 20 C_7N aminoacyclitol metabolites, or its keto analogue-containing metabolites, have been described to date, it appears likely that some of the unknown loci described herein might constitute new classes of C_7N aminoacyclitol, or of its keto analogue-containing metabolites. As these metabolites, some of which contain valienamine, are among the most potent antidiabetic agents thus far discovered, the molecular detection of specific metabolite-producing actinomycetes may prove a crucial step in current attempts to expand the scope and diversity of natural-product discovery.
- Isolation and Characterization of a-Glucosidase Inhibitor from the Fungus Ganoderma lucidum
- Shin-Duk Kim , Hong Joon Nho
- J. Microbiol. 2004;42(3):223-227.
- DOI: https://doi.org/2085 [pii]
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Abstract
- An [alpha]-glucosidase inhibitor, SKG-3, was isolated from the fruiting bodies of Ganoderma lucidum and its physico-chemical properties were characterized. It was a highly specific and effective reversible inhibitor of [alpha]-glucosidase. It showed very potent inhibitory activity against [alpha]-glucosidase with an IC_50 value of 4.6 mg/ml, but no activity for any other glycosidases tested. Enzyme activity could be recovered upon dialysis, thus providing evidence for the reversibility of the inhibition. A Lineweaver-Burk plot indicated that the SKG-3 inhibition of [alpha]-glucosidase was competitive.
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