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Literature summary extracted from

  • Chowdhury, S.; Thomas, M.G.; Escalante-Semerena, J.C.; Banerjee, R.
    The coenzyme b12 analog 5'-deoxyadenosylcobinamide-gdp supports catalysis by methylmalonyl-coa mutase in the absence of trans-ligand coordination (2001), J. Biol. Chem., 276, 1015-1019.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.2 expression in Escherichia coli 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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4.99.2 18
-
(R)-2-methylmalonyl-CoA 30°C, with 5'-deoxyadenosylcobinamide GDP as cofactor Propionibacterium freudenreichii subsp. shermanii
5.4.99.2 73
-
(R)-2-methylmalonyl-CoA 30°C, with 5'-adenosylcobalamin as cofactor Propionibacterium freudenreichii subsp. shermanii

Cofactor

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