N-acylsphingosine Galactosyltransferase
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N-acylsphingosine Galactosyltransferase
In enzymology, a N-acylsphingosine galactosyltransferase () is an enzyme that catalysis, catalyzes the chemical reaction :UDP-galactose + N-acylsphingosine \rightleftharpoons UDP + D-galactosylceramide Thus, the two substrate (biochemistry), substrates of this enzyme are UDP-galactose and N-acylsphingosine, whereas its two product (chemistry), products are uridine diphosphate, UDP and D-galactosylceramide. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The List of enzymes, systematic name of this enzyme class is UDP-galactose:N-acylsphingosine D-galactosyltransferase. Other names in common use include UDP galactose-N-acylsphingosine galactosyltransferase, and uridine diphosphogalactose-acylsphingosine galactosyltransferase. This enzyme participates in sphingolipid metabolism. References

* EC 2.4.1 Enzymes of unknown structure {{2.4-enzyme-stub ...
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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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