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Literature summary extracted from

  • Allen, S.H.; Kellermeyer, R.W.; Stjernholm, R.L.; Wood, H.G.
    Purification and properties of enzymes involved in the propionic acid fermentation (1964), J. Bacteriol., 87, 171-187 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.27 0.068
-
 succinyl-CoA with propanoate as cosubstrate, at pH 7.8 and 25°C Propionibacterium freudenreichii subsp. shermanii
2.8.3.27 0.13
-
 succinyl-CoA with acetate as cosubstrate, at pH 8.0 and 25°C Propionibacterium freudenreichii subsp. shermanii
2.8.3.27 0.62
-
 propanoate at pH 7.8 and 25°C Propionibacterium freudenreichii subsp. shermanii
2.8.3.27 7
-
 acetate with acetate as cosubstrate, at pH 8.0 and 25°C Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.27 Propionibacterium freudenreichii subsp. shermanii
-
-
-
2.8.3.27 Propionibacterium freudenreichii subsp. shermanii 52W
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.27 DEAE column chromatography and TEAE cellulose column chromatography, and ammonium sulfate precipitation Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.27 acetate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii acetyl-CoA + succinate
-
 r
2.8.3.27 acetate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii 52W acetyl-CoA + succinate
-
 r
2.8.3.27 additional information the enzyme does not catalyse the transfer of CoA from succinyl-CoA to acetoacetate. The enzyme does not catalyse the transfer of CoA from acetyl-CoA to methylmalonate, acetoacetate, formate, or fluoroacetate, or from 3-hydroxy-3-methylglutaryl-CoA to acetate Propionibacterium freudenreichii subsp. shermanii ?
-
-
2.8.3.27 additional information the enzyme does not catalyse the transfer of CoA from succinyl-CoA to acetoacetate. The enzyme does not catalyse the transfer of CoA from acetyl-CoA to methylmalonate, acetoacetate, formate, or fluoroacetate, or from 3-hydroxy-3-methylglutaryl-CoA to acetate Propionibacterium freudenreichii subsp. shermanii 52W ?
-
-
2.8.3.27 propanoate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii propanoyl-CoA + succinate
-
 r
2.8.3.27 propanoate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii 52W propanoyl-CoA + succinate
-
 r
2.8.3.27 propanoyl-CoA + succinate
-
 Propionibacterium freudenreichii subsp. shermanii propanoate + succinyl-CoA
-
 r
2.8.3.27 propanoyl-CoA + succinate
-
 Propionibacterium freudenreichii subsp. shermanii 52W propanoate + succinyl-CoA
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.8.3.27 CoA transferase
-
 Propionibacterium freudenreichii subsp. shermanii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.3.27 6.5 7.8
-
 Propionibacterium freudenreichii subsp. shermanii