Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Swick, R.W.; Wood, H.G.
    The role of transcarboxylase in propionic acid ermentation (1960), Proc. Natl. Acad. Sci. USA, 46, 28-41.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.1 Avidin biotin restores Propionibacterium freudenreichii subsp. shermanii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.3.1 cytoplasm
-
Canis lupus familiaris 5737
-
2.1.3.1 cytoplasm
-
Propionibacterium freudenreichii subsp. shermanii 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.3.1 Co2+ requirement Canis lupus familiaris
2.1.3.1 Co2+ requirement Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Canis lupus familiaris
-
-
-
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
-
-
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii 52W
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1 partially Propionibacterium freudenreichii subsp. shermanii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.3.1 additional information not ox liver Canis lupus familiaris
-
2.1.3.1 skeletal muscle not heart muscle Canis lupus familiaris
-

Storage Stability

EC Number Storage Stability Organism
2.1.3.1 -12°C, partially purified at least 1 month Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.1 acetoacetyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii 3-oxoglutaryl-CoA + pyruvate
-
?
2.1.3.1 acetoacetyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii 52W 3-oxoglutaryl-CoA + pyruvate
-
?
2.1.3.1 acetyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii malonyl-CoA + pyruvate
-
?
2.1.3.1 acetyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii 52W malonyl-CoA + pyruvate
-
?
2.1.3.1 butyryl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii ethylmalonyl-CoA + pyruvate
-
?
2.1.3.1 butyryl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii 52W ethylmalonyl-CoA + pyruvate
-
?
2.1.3.1 additional information
-
Canis lupus familiaris ?
-
?
2.1.3.1 additional information structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A Propionibacterium freudenreichii subsp. shermanii ?
-
?
2.1.3.1 additional information structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A Propionibacterium freudenreichii subsp. shermanii 52W ?
-
?
2.1.3.1 propionyl-CoA + oxaloacetate
-
Canis lupus familiaris (S)-methylmalonyl-CoA + pyruvate
-
r
2.1.3.1 propionyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
r
2.1.3.1 propionyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii 52W (S)-methylmalonyl-CoA + pyruvate
-
r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.1 30
-
assay at Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 additional information no ATP requirement Propionibacterium freudenreichii subsp. shermanii