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Literature summary extracted from

  • Rivera-Hainaj, R.E.; Pusztai-Carey, M.; Reddy, D.V.; Choowongkomon, K.; Soennichsen, F.D.; Carey, P.R.
    Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies (2002), Biochemistry, 41, 2191-2197.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.1 1.3S subunit cloned and expressed in Escherichia coli 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 enzyme and mutant 1.3S subunit 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 spontaneous decarboxylation follows Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
r

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.3.1 additional information
-
effect of pH on the overall conformation of the 1.3 subunit, below 3.5 and above 9.0: the N-terminus of the 1.3S protein undergoes a transition into a random coil or unordered conformation 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 biotin covalently linked to the 1.3 subunit to the epsilon-amino group of Lys-89, which lies in the conserved sequence Ala-Met-Lys-Met Propionibacterium freudenreichii subsp. shermanii