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Literature summary for 6.3.4.9 extracted from

  • Lane, M.D.; Rominger, K.L.; Young, D.L.; Lynene, F.
    The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. II. INVESTIGATION OF THE REACTION MECHANISM. (1964), J. Biol. Chem., 239, 2865-2871.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00042
-
(+)-biotin
-
Propionibacterium freudenreichii subsp. shermanii

Organism

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

Reaction

Reaction Comment Organism Reaction ID
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase] mechanism, (+)-biotinyl-5'-AMP is an intermediate in holotranscarboxylase synthesis Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase] specific for (+)-biotin Propionibacterium freudenreichii subsp. shermanii AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
-
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