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

BRENDA support

Literature summary for 5.4.99.2 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
Search for more literature for 5.4.99.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli 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

Turnover Number [1/s]

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

Cofactor

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