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Literature summary for 2.1.3.1 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)

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

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

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

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
(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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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
2.3
-
recombinant 5S subunit, overall reaction Propionibacterium freudenreichii subsp. shermanii
48
-
5S subunit, overall reaction Propionibacterium freudenreichii subsp. shermanii
323
-
5S subunit, partial reaction 2 Propionibacterium freudenreichii subsp. shermanii
330
-
recombinant 5S subunit, partial reaction 2 Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
More 5S subunit with a native MW 120000 Da, gel filtration and a subunit MW 60000 Da, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii
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

Cofactor Comment Organism Structure
biotin requirement Propionibacterium freudenreichii subsp. shermanii