SUMMARY: A new strain of pink facultative methylotroph, bacterium AT2, capable of growth on methylamine, trimethylamine, methanol, formate and a range of non-C substrates has been isolated. On the basis of the enzyme activities in cell-free extracts, the organism appears to have the same pathway for trimethylamine oxidation as , i.e. via trimethylamine -oxide and -methylglutamate. -Methylglutamate dehydrogenase in this organism was a ‘soluble’ enzyme (i.e. was not sedimented at 100000 in 60 min) and reacted with the electron acceptors phenazine methosulphate, 2,6-dichlorophenolindophenol, Wurster's blue and the radical cation of 2,2'-azinodi-[3-ethylbenzthiazoline 6-sulphonate]. It was not active with NAD, ferricyanide or cytochrome The enzyme was purified to apparent homogeneity (as assessed by polyacrylamide gel electrophoresis) and was shown to contain flavin and cytochrome , both of which could be reduced by -methylglutamate. The flavin prosthetic group could be liberated by boiling and was probably FAD. The true of the enzyme for -methylglutamate was 0·33 m and for 2,6-dichlorophenolindophenol, 0·20 m.


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