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.
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 |
|