Species: Aminobacter aminovorans
Cells of Aminobacter aminovorans grown on methylamine, dimethylamine, trimethylamine or trimethylamine N-oxide, but not on other carbon sources, contain a particle-bound methylglutamate dehydrogenase. Membranes containing the enzyme could catalyze an N-methyl-L-glutamate-dependent uptake of molecular oxygen and were able to reduce cytochrome c. The partially-purified enzyme (145-fold), assayed with artificial electron acceptors, was also active with sarcosine, N-methyl-L-alanine and N-methyl-DL-aspartate, and was able to accept N-methyl D-amino acids [Bamforth77].
Earlier work reported that neither glutamate nor formaldehyde inhibit the enzyme, and suggested that the actual product may be N-methylene glutamate rather than glutamate andr formaldehyde [Hersh72]. However, subsequent research found that formaldehyde was indeed an inhibitor [Bamforth77].
Enzymatic reaction of: methylglutamate dehydrogenase
EC Number: 220.127.116.11N-methyl-L-glutamate + an oxidized unknown electron acceptor + H2O → L-glutamate + formaldehyde + an reduced unknown electron acceptor
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.Alternative Substrates for N-methyl-L-glutamate: N-methyl-DL-aspartate [Bamforth77], sarcosine [Bamforth77], N-methyl-L-alanine [Bamforth77] p-chloromercuribenzoate [Bamforth77], iodoacetamide [Bamforth77] Inhibitors (Unknown Mechanism): formaldehyde [Bamforth77], 2-oxoglutarate [Bamforth77]Kinetic Parameters:
pH(opt): 6.5 [Bamforth77]
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