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- W2077689323 abstract "Abstract The occurence of a substrate-unspecific l -leucine carboxylyase in marine red algae has been demonstrated. The enzyme was found to occur in 13 out of 27 species tested. The very stable enzyme appears to be firmly particle-bound. All attempts to demonstrate activity in solution so far failed. Preparations obtained by acetone-treatment of fresh or preserved algae, which were further purified by exhaustive aqueous extraction were found suitable for detailed enzyme studies. The enzymic reactions have distinct pH optima in the range of 4·25 to 6·0. The precise values depend on the algal species the enzymes are derived from. In addition to leucine, the following amino acids were decarboxylated: norleucine, isoleucine, valine, norvaline, 2-aminobutyric acid, alanine, 2-aminoheptanoic acid, phenylalanine, methionine, cysteine, homocysteine. it has been confirmed that all these substrates are decarboxylated by a single enzyme. With two exceptions pyridoxalphosphate (PALP) was necessary to obtain full activity. But even in the presence of PALP an unusual substrate-dependent inactivation occurs. This inactivation was highest in fresh preparations but decreased during the storage of enzymic material." @default.
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- W2077689323 date "1972-04-01" @default.
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- W2077689323 title "Leucin-carboxylyase aus marinen rhodophyceae: Vorkommen, verbreitung und einige eigenschaften" @default.
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- W2077689323 doi "https://doi.org/10.1016/s0031-9422(00)90081-5" @default.
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