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Literature summary for 4.1.1.38 extracted from

  • O'Brien, W.E.; Wood, H.G.
    Carboxytransphosphorylase. 8. Ligand-mediated interaction of subunits as a possible control mechanism in Propionibacteria (1974), J. Biol. Chem., 249, 4917-4925.
    View publication on PubMed
Search for more literature for 4.1.1.38

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
 monomeric enzyme form,equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii
224000
-
 dimeric enzyme form, equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii
378000
-
 tetrameric enzyme form, equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphate + phosphoenolpyruvate + CO2 Propionibacterium freudenreichii subsp. shermanii ligand induced subunit interactions play a role in the control of the propionic acid fermentation ?
-
 ?

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphate + phosphoenolpyruvate + CO2
-
 Propionibacterium freudenreichii subsp. shermanii diphosphate + oxaloacetate
-
 r
phosphate + phosphoenolpyruvate + CO2 ligand induced subunit interactions play a role in the control of the propionic acid fermentation Propionibacterium freudenreichii subsp. shermanii ?
-
 ?
phosphoenolpyruvate + phosphate
-
 Propionibacterium freudenreichii subsp. shermanii pyruvate + diphosphate
-
 ir

Subunits

Subunits Comment Organism
dimer 2 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii
monomer 1 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii
More the dissociation of the tetrameric enzyme and association of monomeric enzyme to dimeric forms occurs during catalysis of the forward reaction, caused by the product oxaloacetate, or by malate or fumarate. The monomeric form and the dimeric form are less active than the tetrameric enzyme form Propionibacterium freudenreichii subsp. shermanii
tetramer 4 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation Propionibacterium freudenreichii subsp. shermanii