Abstract
The antibiotic pentalenolactone, isolated from the fermentation broth of various species of Streptomyces1–3, has three different forms depending on culture conditions and purification procedure: E (epoxide; Fig. 1), D (diol) and C (chlorhydrine). The latter two derive from E by cleavage of the epoxide ring with insertion of the elements of water and HCl, respectively. As in vitro studies have shown6, pentalenolactone inhibits glycolysis by inhibiting specifically glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but no other enzyme was known to be affected. The inhibition is irreversible and is similar whether the enzyme comes from Escherichia coli, yeast or rabbit muscle. We report here that the antibiotic has different effects on the three classes of glyceraldehyde-3-phosphate dehydrogenases that occur in spinach leaves, and we demonstrate its high specificity for the glycolytic enzyme.
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Mann, K., Mecke, D. Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenases by pentalenolactone. Nature 282, 535–536 (1979). https://doi.org/10.1038/282535a0
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DOI: https://doi.org/10.1038/282535a0
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