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- W2067571365 abstract "Conversion of leucine to isovaleric (iV) and isocaproic (iC) acids by cell-free extracts of Clostridium bifermentans was demonstrated using two lysis procedures. Sonication resulted in an extract which had the enzymes to convert leucine to α-ketoisocaproic acid (α-kiC) and thence iV, but failed to produce iC. Extracts prepared by osmotic lysis, which contained intact membranes, could convert leucine to both iV and iC. The enzyme which converts leucine to α-kiC was solubilized during osmotic lysis, whereas the decarboxylase and leucine reductase system remained membrane bound. Osmotic lysis also released at least two small molecular weight, heat-stable, anionic components (3500 > molecular weight [Formula: see text] 1000), which stimulated decarboxylase activity." @default.
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- W2067571365 date "1983-04-01" @default.
- W2067571365 modified "2023-09-23" @default.
- W2067571365 title "Subcellular location of enzymes involved in leucine dissimilation in Clostridium bifermentans" @default.
- W2067571365 doi "https://doi.org/10.1139/m83-071" @default.
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