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

EC Number:

N-methyl-L-glutamate + an oxidized unknown electron acceptor + H2O <=> L-glutamate + formaldehyde + an reduced unknown electron acceptor

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.

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:

Km (μM)

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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