MetaCyc Enzyme: methylglutamate dehydrogenase

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].

Locations: membrane

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Cellular Component:
GO:0016020 - membrane [Bamforth77]

Created 08-Dec-2011 by Caspi R, SRI International

Enzymatic reaction of: methylglutamate dehydrogenase

Inferred from experiment

EC Number:

N-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]

In Pathways: superpathway of trimethylamine degradation, methylamine degradation II

Inhibitors (Other): p-chloromercuribenzoate [Bamforth77], iodoacetamide [Bamforth77] Inhibitors (Unknown Mechanism): formaldehyde [Bamforth77], 2-oxoglutarate [Bamforth77]Kinetic Parameters:
Substrate Km (μM) Citations
N-methyl-L-alanine 25000.0 [Bamforth77]
N-methyl-L-glutamate 25.0 [Bamforth77]

pH(opt): 6.5 [Bamforth77]


Bamforth77: Bamforth CW, Large PJ (1977). "Solubilization, partial purification and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans." Biochem J 161(2);357-70. PMID: 15545

Hersh72: Hersh LB, Stark MJ, Worthen S, Fiero MK (1972). "N-methylglutamate dehydrogenase: kinetic studies on the solubilized enzyme." Arch Biochem Biophys 150(1);219-26. PMID: 5028076

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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