BRENDA - Enzyme Database

Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli

No, Z.; Sanders, C.R.; Dowhan, W.; Tsai, M.D.; Bioorg. Chem. 16, 184-188 (1988)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
4.1.1.65
pyruvate
dependent on
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.1.1.65
membrane
bound to
Escherichia coli
16020
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.1.65
Escherichia coli
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
4.1.1.65
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
reaction is completely stereospecific with overall retention of configuration
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.65
Phosphatidyl-L-serine
-
4780
Escherichia coli
Phosphatidylethanolamine + CO2
-
4780
Escherichia coli
-
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
4.1.1.65
pyruvate
dependent on
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.1.1.65
membrane
bound to
Escherichia coli
16020
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.65
Phosphatidyl-L-serine
-
4780
Escherichia coli
Phosphatidylethanolamine + CO2
-
4780
Escherichia coli
-