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Literature summary extracted from

  • Schulman, M.; Wood, H.
    Succinyl-CoA propionate CoA-transferase from Propionibacterium shermanii EC 2.8.3.6 succinyl-CoA propionate CoA-transferase (1975), Methods Enzymol., 35, 235-242 .
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.27 0.0625
-
 propanoate at pH 8.0 and 25°C Propionibacterium freudenreichii subsp. shermanii
2.8.3.27 0.068
-
 succinyl-CoA 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-cellulose column chromatography, cellulose phosphate column chromatography, ammonium sulfate fractionation, TEAE-cellulose column chromatography, and Sephadex G-200 gel filtration Propionibacterium freudenreichii subsp. shermanii

Storage Stability

EC Number Storage Stability Organism
2.8.3.27 -20°C, 0.1 M phosphate (pH 6.8) containing 0.1 mM EDTA, the enzyme is quite stable at protein concentrations greater than 1 mg/ml, approximately, a 30% loss of enzymatic activity occurs during 1 year Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.27 additional information the enzyme can also use acetate and acetyl-CoA as substrate instead of propionate and propanoyl-CoA, respectively. The enzyme does not catalyze transfer from acetyl-CoA to methylmalonate, from beta-hydroxy-beta-methylglutaryl-CoA to acetate or from acetoacetyl-CoA to succinate Propionibacterium freudenreichii subsp. shermanii ?
-
-
2.8.3.27 additional information the enzyme can also use acetate and acetyl-CoA as substrate instead of propionate and propanoyl-CoA, respectively. The enzyme does not catalyze transfer from acetyl-CoA to methylmalonate, from beta-hydroxy-beta-methylglutaryl-CoA to acetate or from acetoacetyl-CoA to succinate 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 succinyl-CoA: propionate CoA-transferase
-
 Propionibacterium freudenreichii subsp. shermanii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.8.3.27 6.5 8 the enzyme has a broad optimum between pH 6.5 and 8.0, 50% activity at pH 5.5. There is no enzymatic activity at pH 8.5 Propionibacterium freudenreichii subsp. shermanii