Literature summary for 4.1.1.65 extracted from

Li, Q.X.; Dowhan, W.
Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli (1990), J. Biol. Chem., 265, 4111-4115.

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Protein Variants

Protein Variants	Comment	Organism
S254C	mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase	Escherichia coli
S254T	mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Phosphatidyl-L-serine	-	Escherichia coli	Phosphatidylethanolamine + CO2	-	?

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Release 2023.1 (January 2023)