Literature summary for 6.4.1.1 extracted from

Westerhold, L.E.; Adams, S.L.; Bergman, H.L.; Zeczycki, T.N.
Pyruvate occupancy in the carboxyl transferase domain of pyruvate carboxylase facilitates product release from the biotin carboxylase domain through an intermolecular mechanism (2016), Biochemistry, 55, 3447-3460 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	generation of functional, mixed hybrid tetramers using the E218A (inactive biotin carboxylase domain) and T882S (low pyruvate binding, low activity) mutant forms of pyruvate carboxylase. The apparent Ka pyruvate for the pyruvate-stimulated release of Pi by the hybrid tetramer is comparable to the wild-type enzyme and nearly 10fold lower than that for the T882S homotetramer. The ratio of the rates of oxaloacetate formation to Pi release for the WT:T882S[1:1] complex and 218A:T882S[1:1] hybrid tetramer-catalyzed reactions is 0.5 and 0.6, respectively, while the T882S homotetramer exhibits a near 1:1 coupling of the two domains	Rhizobium etli

Organism

Organism	UniProt	Comment	Textmining
Rhizobium etli	Q2K340	-	-
Rhizobium etli ATCC 51251	Q2K340	-	-

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Release 2023.1 (January 2023)