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Literature summary for 2.1.3.1 extracted from

  • Woo, S.B.; Shenoy, B.C.; Wood, H.G.; Magner, W.J.; Kumar, G.K.; Beegen, H.; Samols, D.
    Effect of deletion from the carboxyl terminus of the 12 S subunit on activity of transcarboxylase (1993), J. Biol. Chem., 268, 16413-16419.
    View publication on PubMed
Search for more literature for 2.1.3.1

Cloned(Commentary)

Cloned (Comment) Organism
12S subunit cloned and expressed in Escherichia coli 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
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification 97 amino acids deleted of the carboxyl-terminal region of the monomer of the 12S subunit, 46% loss of activity because of a reduces stability of the 12S subunit and a decrease in binding of 6S subunit to the 12 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
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 comparison of wild-type and truncated forms 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

Cofactor

Cofactor Comment Organism Structure
biotin requirement Propionibacterium freudenreichii subsp. shermanii