Literature summary for 2.1.3.1 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
1.3S subunit cloned and expressed in Escherichia coli	Propionibacterium freudenreichii subsp. shermanii

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme and mutant 1.3S subunit	Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
propionyl-CoA + oxaloacetate	spontaneous decarboxylation follows	Propionibacterium freudenreichii subsp. shermanii	(S)-methylmalonyl-CoA + pyruvate	-	r

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
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

Cofactor	Comment	Organism	Structure
biotin	requirement	Propionibacterium freudenreichii subsp. shermanii
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

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Release 2023.1 (January 2023)