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Literature summary extracted from

  • Xie, Y.; Shenoy, B.C.; Magner, W.J.; Hejlik, D.P.; Samols, D.
    Purification and characterization of the recombinant 5 S subunit of transcarboxylase from Escherichia coli (1993), Protein Expr. Purif., 4, 456-464.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.1 5S subunit cloned and expressed in Escherichia coli Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.3.1 Co2+ necessary for 5S activity Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 Zn2+ necessary for 5S activity Propionibacterium freudenreichii subsp. shermanii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.1 120000
-
 the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000 Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1 recombinant 5S subunit Propionibacterium freudenreichii subsp. shermanii

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate partial reaction 1 is catalysed specifically by the 12S subunit, partial reaction 2 is catalysed specifically by the 5S subunit Propionibacterium freudenreichii subsp. shermanii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.1 additional information
-
 the recombinant 5S subunit is active in partial reaction 2 but not in overall enzyme reaction and not able to form a enzyme complex Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 2.3
-
 recombinant 5S subunit, overall reaction Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 48
-
 5S subunit, overall reaction Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 323
-
 5S subunit, partial reaction 2 Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 330
-
 recombinant 5S subunit, partial reaction 2 Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.1 propionyl-CoA + oxaloacetate two partial reactions Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
 r

Subunits

EC Number Subunits Comment Organism
2.1.3.1 More the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000 Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 More 5S subunit with a native MW 120000 Da, gel filtration and a subunit MW 60000 Da, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 More 5S subunit is a dimer of identical monomers, contains Co2+ and Zn2+ and assembles with two 1.3 subunits to form a stable complex termed the 6S subunit Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii