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Arnold L. Demain
Researcher at Drew University
Publications - 425
Citations - 21576
Arnold L. Demain is an academic researcher from Drew University. The author has contributed to research in topics: Streptomyces clavuligerus & Clostridium thermocellum. The author has an hindex of 66, co-authored 424 publications receiving 20140 citations. Previous affiliations of Arnold L. Demain include Massachusetts Institute of Technology & Merck & Co..
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ATP and adenylate enegry charge during phosphate-mediated control of antibiotic synthesis
TL;DR: The addition of inorganic phosphate or guanosine-5′-monophosphate to a phosphate-limited mycelial system of Streptomyces griseus inhibited candicidin production and Adenylate energy charge increased only slightly indicating that ATP is a more likely intracellular effector than energy charge in mediating phosphate control of antibiotic biosynthesis.
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Lysine control of penicillin biosynthesis
TL;DR: The known diminution in penicillin formation by added lysine is thought to occur via feedback regulation of the lysin biosynthetic pathway, thus depleting the cells of α-aminoadipic acid, a precur...
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Carbon source regulation of cephem antibiotic production by resting cells of Streptomyces clavuligerus and its reversal by protein synthesis inhibitors
TL;DR: The effect of utilizable carbon sources on the production of cephem antibiotics by Streptomyces clavuligerus has been studied and Glycerol, maltose and starch supported the most extensive growth.
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The cyclohexane moiety of rapamycin is derived from shikimic acid in Streptomyces hygroscopicus
TL;DR: It was found that 13C-shikimic acid was incorporated into the cyclohexane moiety of rapamycin, thereby establishing the shikIMic acid pathway origin of the seven-carbon starter unit.
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Synthesis of bacilysin by Bacillus subtilis branches from prephenate of the aromatic amino acid pathway.
TL;DR: Previously characterized mutants of Bacillus subtilis 168 were analyzed for the accumulation of the antibiotic bacilysin in culture broths and for the presence of b Bacilysin synthetase in cell extracts, suggesting that prephenate is the primary metabolic precursor of bacallysin.