Purification and Some Properties of 2, 6-Diaminopimelate Decarboxylase from Rumen Protozoon, Entodinium caudatum

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  • ルーメンプロトゾァEntodinium caudatumの2,6-ジアミノピメリン酸脱炭酸酵素の精製および諸性質

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Abstract

Diaminopimelate decarboxylase (EC4.1.1.20) from a cell free extract of a rumen protozoon Entodinium caudatum was purified 430-folds by ammonium sulphate precipitation and column chromatography with hydroxylapatite, DEAE-cellulose and sephadex G-150. The molecular weight of the enzyme was estimated to be 54, 000 by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH for catalytic activity of the purified enzyme from E. caudatum was found to be 6.3 and catalytic activities were retained between 5.0 and 6.8. The optimal temperature was 50°C. The enzyme was stable at below 60°C and the activity was completely lost at 65°C. For the stability of the enzyme the presence of pyridoxal 5'-phosphate (PLP) and thiol group such as 2-mercaptoethanol and dithiothreitol were necessary. PLP was the only pyridoxine derivative which acted as a cofactor. The Michaelis constant (Km) of this enzyme for 2, 6-diaminopimelate was 0.8mM.

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