Literature summary for 4.1.1.49 extracted from

Cannata, J.J.B.; de Flombaum, M.A.C.
Phosphopyruvate carboxykinase from baker' yeast. Kinetics of phosphoenolpyruvate formation (1974), J. Biol. Chem., 249, 3356-3365.

Search for more literature for 4.1.1.49

Inhibitors

Inhibitors	Comment	Organism	Structure
ATP	excess of ATP over MnCl2 is inhibitory	Saccharomyces cerevisiae
MnCl2	excess ogf MnCl2 over ATP is inhibitory	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cd2+	can fulfill the free divalent cation requirement	Saccharomyces cerevisiae
Mn2+	can fulfill the free divalent cation requirement	Saccharomyces cerevisiae
additional information	enzyme contains at least two binding sites, related to cation requirement. One binding a cation-nucleotide complex, the true substrate, and the latter site greatly enhances the affinity of the former for the cation nucleotide substrate	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphoenolpyruvate + CO2	-	Saccharomyces cerevisiae	ATP + oxaloacetate	-	?

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	oxaloacetate formation	Saccharomyces cerevisiae
8.3	-	phosphoenolpyruvate formation	Saccharomyces cerevisiae

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.3	7.5	pH 5.3: about 30% of maximal activity, pH 7.5: about 25% of maximal activity, oxaloacetate formation	Saccharomyces cerevisiae
6.3	9.3	pH 6.3: about 35% of maximal activity, pH 9.3: about 30% of maximal activity, phosphoenolpyruvate formation	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)