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Literature summary extracted from

  • Kung, H.F.; Tsai, L.
    Nicotinic acid metabolism. VII. Mechanism of action of Clostridial alpha-methyleneglutarate mutase (B12-dependent) and methylitaconate isomerase (1971), J. Biol. Chem., 246, 6436-6443.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.3.6 Methylitaconate Eubacterium barkeri key step in the overall fermentation of nicotinate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.6 Eubacterium barkeri
-
-
-
5.4.99.4 Eubacterium barkeri
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.99.4 2-Methyleneglutarate = 2-methylene-3-methylsuccinate mechanism Eubacterium barkeri
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.3.6 culture condition:nicotinic acid-grown cell not detectable in cells grown on glucose Eubacterium barkeri
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.3.6 Methylitaconate r Eubacterium barkeri Dimethylmaleate
-
 ?
5.3.3.6 Methylitaconate formation of dimethylmaleate is favored Eubacterium barkeri Dimethylmaleate
-
 ?
5.3.3.6 Methylitaconate key step in the overall fermentation of nicotinate Eubacterium barkeri ?
-
 ?
5.4.99.4 2-Methyleneglutarate
-
 Eubacterium barkeri 2-Methylene-3-methylsuccinate i.e methylitaconate ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.4 vitamin B12 dependent on Eubacterium barkeri