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Literature summary for 2.8.3.27 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
Search for more literature for 2.8.3.27

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0625
-
 propanoate at pH 8.0 and 25°C Propionibacterium freudenreichii subsp. shermanii
0.068
-
 succinyl-CoA at pH 8.0 and 25°C Propionibacterium freudenreichii subsp. shermanii

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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

Storage Stability Organism
-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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
-
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 ?
-
-
propanoate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii propanoyl-CoA + succinate
-
 r
propanoate + succinyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii 52W propanoyl-CoA + succinate
-
 r
propanoyl-CoA + succinate
-
 Propionibacterium freudenreichii subsp. shermanii propanoate + succinyl-CoA
-
 r
propanoyl-CoA + succinate
-
 Propionibacterium freudenreichii subsp. shermanii 52W propanoate + succinyl-CoA
-
 r

Synonyms

Synonyms Comment Organism
succinyl-CoA: propionate CoA-transferase
-
 Propionibacterium freudenreichii subsp. shermanii

pH Range

pH Minimum pH Maximum Comment Organism
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