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Literature summary for 5.4.99.2 extracted from

  • Francalanci, F.; Davis, N.K.; Fuller, J.Q.; Murfitt, D.; Leadlay, P.F.
    The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii (1986), Biochem. J., 236, 489-494.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67000
-
1 * 67000 + 1 * 79000, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii
79000
-
1 * 67000 + 1 * 79000, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii
163000 165000 sedimentation equilibrium analysis, gel filtration Propionibacterium freudenreichii subsp. shermanii

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionibacterium freudenreichii subsp. shermanii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-methylmalonyl-CoA
-
Propionibacterium freudenreichii subsp. shermanii succinyl-CoA
-
?

Subunits

Subunits Comment Organism
dimer 1 * 67000 + 1 * 79000, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii

Cofactor

Cofactor Comment Organism Structure
cobamide dependent on Propionibacterium freudenreichii subsp. shermanii