Literature summary for 4.1.1.31 extracted from

Duff, S.M.G.; Lepiniec, L.; Cretin, C.; Andreo, C.S.; Condon, S.A.; Sarath, G.; Vidal, J.; Gadal, P.; Chollet, R.
An engineered change in the L-malate sensitivity of a site-directed mutant of Sorghum phosphoenolpyruvate carboxylase: the effect of sequential mutagenesis and S-carboxymethylation at position 8 (1993), Arch. Biochem. Biophys., 306, 272-276.

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Protein Variants

Protein Variants	Comment	Organism
S8C	he S-carboxymethylated S8C mutant enzyme, in contrast to the SH-modified wild type protein, has an increased I0.5 value for L-malate similar to that of the phosphorylated Ser8 enzyme and the S8D mutant protein	Sorghum sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Sorghum sp.

Organism

Organism	UniProt	Comment	Textmining
Sorghum sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild type and mutant enzymes S8C, and S8D	Sorghum sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phosphoenolpyruvate + CO2	-	Sorghum sp.	phosphate + oxaloacetate	-	?

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Release 2023.1 (January 2023)