1979 年 43 巻 6 号 p. 1197-1203
A sarcosine dehydrogenase was purified to homogeneity from cell free extract of Pseudomanas putida aerobically grown in a medium containing creatinine or betaine as the carbon and nitrogen sources. The enzyme catalyzed dehydrogenation of N-methyl derivatives of some amino acids but was inert toward dimethylglycine, betaine and choline. Phenazine methosulfate, 2, 6-dichlorophenol indophenol, methylene blue, meldora blue, nile blue and potassium ferricyanide served as electron carriers. The maximal activity was observed at pH 8.0_??_9.0. The Km and Vmax values for sarcosine were 29 mM and 1.2 μmol/min/mg, respectively. The molecular weight was estimated to be about 170, 000, presumably composed of four sub-units. Spectrophotometric and fluorometric analyses indicated that the enzyme was a flavoprotein.
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