Literature summary for 4.1.1.31 extracted from

Takahashi-Terada, A.; Kotera, M.; Ohshima, K.; Furumoto, T.; Matsumura, H.; Kai, Y.; Izui, K.
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation (2005), J. Biol. Chem., 280, 11798-11806.

Search for more literature for 4.1.1.31

Activating Compound

Activating Compound	Comment	Organism	Structure
glucose 6-phosphate	activates wild-type enzyme	Zea mays
glycine	allosteric activator	Zea mays

Cloned(Commentary)

Cloned (Comment)	Organism
-	Zea mays

Protein Variants

Protein Variants	Comment	Organism
R183Q	mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected	Zea mays
R183Q/R184Q	mutation results in complete desensitization to glucose 6-phosphate	Zea mays
R184Q	mutation results in complete desensitization to glucose 6-phosphate	Zea mays
R372Q	mutation results in a marked decrease in sensitivity to glucose 6-phosphate	Zea mays

Inhibitors

Inhibitors	Comment	Organism	Structure
L-malate	inhibits wild-type enzyme	Zea mays

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant	Zea mays

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phosphoenolpyruvate + HCO3-	-	Zea mays	phosphate + oxaloacetate	-	?

Synonyms

Synonyms	Comment	Organism
PEPC	-	Zea mays

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Release 2023.1 (January 2023)