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].
|Cellular Component:||GO:0016020 - membrane [Bamforth77]|
Enzymatic reaction of: methylglutamate dehydrogenase
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
pH(opt): 6.5 [Bamforth77]
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493