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Literature summary for 5.4.99.4 extracted from

  • Pierik, A.J.; Ciceri, D.; Lopez, R.F.; Kroll, F.; Broker, G.; Beatrix, B.; Buckel, W.; Golding, B.T.
    Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri (2005), Biochemistry, 44, 10541-10551.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D483N 0.06%of wild-type activity Eubacterium barkeri
H464Q 35% of wild-type activity Eubacterium barkeri
H485Q less than 0.03% of wild-type activity Eubacterium barkeri

Inhibitors

Inhibitors Comment Organism Structure
1-methylcyclopropane-(1R,2R)-dicarboxylate weak noncompetitive Eubacterium barkeri
additional information acrylate and 2-methylpent-2-enedioate are noninhibitory Eubacterium barkeri

Organism

Organism UniProt Comment Textmining
Eubacterium barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Eubacterium barkeri

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-Methyleneglutarate
-
Eubacterium barkeri 2-Methylene-3-methylsuccinate
-
?

Cofactor

Cofactor Comment Organism Structure
vitamin B12
-
Eubacterium barkeri

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
13
-
1-methylcyclopropane-(1R,2R)-dicarboxylate
-
Eubacterium barkeri