Abstract
Summary: Cells of Citrobacter freundii IFO 12681 contained glutathionylspermidine at a level of 2–3 nmol (g wet cells)−1. Three kinds of enzymes (E1, E2 and E3) catalysing the degradation of glutathionylspermidine were found in extracts of the bacterium. E1 was a spermidine dehydrogenase and was induced by spermidine. The enzyme hydrolysed glutathionylspermidine only in the presence of an electron acceptor. E2 and E3 were formed constitutvely and required no cofactor for the degradation of glutathionylspermidine. E3 required at least two protein components for activity. The reaction products formed by E1, E2 and E3 differed from each other, but have not yet been identified. No activity generating glutathione and spermidine from glutathionylspermidine was detected in extracts of C. freundii.
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