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Literature summary extracted from

  • Mancia F.; Evans, P.R.
    Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism (1998), Structure, 6, 711-720.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.2 overexpression in Escherichia coli Propionibacterium freudenreichii subsp. shermanii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.2 determination of the structure of substrate-free methylmalonyl-CoA mutase is initiated to provide further insight into the mechanism of radical formation Propionibacterium freudenreichii subsp. shermanii
5.4.99.2 vapour diffusion at 23°C Propionibacterium freudenreichii subsp. shermanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.2 (R)-2-methylmalonyl-CoA Propionibacterium freudenreichii subsp. shermanii
-
 succinyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.2 Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.2
-
 Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
5.4.99.2 methylmalonyl-CoA mutase
-
 Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.2 adenosylcobalamin
-
 Propionibacterium freudenreichii subsp. shermanii