Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.99.2 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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
vapour diffusion at 23°C Propionibacterium freudenreichii subsp. shermanii

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
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
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin
-
Propionibacterium freudenreichii subsp. shermanii