Serine-phosphoethanolamine Synthase
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Serine-phosphoethanolamine Synthase
In enzymology, a serine-phosphoethanolamine synthase () is an enzyme that catalysis, catalyzes the chemical reaction :CDP-ethanolamine + L-serine \rightleftharpoons CMP + L-serine-phosphoethanolamine Thus, the two substrate (biochemistry), substrates of this enzyme are CDP-ethanolamine and L-serine, whereas its two product (chemistry), products are cytidine monophosphate, CMP and L-serine-phosphoethanolamine. This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The List of enzymes, systematic name of this enzyme class is CDP-ethanolamine:L-serine ethanolamine phosphotransferase. Other names in common use include serine ethanolamine phosphate synthetase, serine ethanolamine phosphodiester synthase, serine ethanolaminephosphotransferase, serine-phosphinico-ethanolamine synthase, and serinephosphoethanolamine synthase. This enzyme participates in glycerophospholipid metabolism. References

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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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