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Literature summary for 2.7.8.8 extracted from

  • Carman, G.M.; Dowhan, W.
    Phosphatidylserine synthase from Escherichia coli. The role of Triton X-100 in catalysis (1979), J. Biol. Chem., 254, 8391-8397.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100 increasing levels of Triton X-100 at low molecular ratios of Triton X-100 to CDP-diacylglycerol stimulate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Triton X-100 inhibits activity as the molar ratio of Triton X-100 to CDP-diacylglycerol raises beyond the point of maximal activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CDP-diacylglycerol + L-serine Escherichia coli the enzyme catalyzes the first committed step in the biosynthesis of phosphatidylethanolamine CMP + 3-O-sn-phosphatidyl-L-serine
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CDP-diacylglycerol + L-Ser
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Escherichia coli CMP + 3-O-sn-phosphatidyl-L-serine
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CDP-diacylglycerol + L-serine the enzyme catalyzes the first committed step in the biosynthesis of phosphatidylethanolamine Escherichia coli CMP + 3-O-sn-phosphatidyl-L-serine
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additional information the enzyme is specific for the L-glycerol-3-phosphate isomer of the liponucleotide and does not recognize the D-isomer of the 1-monoacyl derivative Escherichia coli ?
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