Ceramide cholinephosphotransferase

Last updated
ceramide cholinephosphotransferase
Identifiers
EC no. 2.7.8.3
CAS no. 9026-14-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a ceramide cholinephosphotransferase (EC 2.7.8.3) is an enzyme that catalyzes the chemical reaction

CDP-choline + N-acylsphingosine CMP + sphingomyelin

Thus, the two substrates of this enzyme are CDP-choline and N-acylsphingosine, whereas its two products are CMP and sphingomyelin.

This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:N-acylsphingosine cholinephosphotransferase. This enzyme is also called phosphorylcholine-ceramide transferase. This enzyme participates in sphingolipid metabolism.

Related Research Articles

<span class="mw-page-title-main">Phospholipid</span> Class of lipids

Phospholipids are a class of lipids whose molecule has a hydrophilic "head" containing a phosphate group and two hydrophobic "tails" derived from fatty acids, joined by an alcohol residue. Marine phospholipids typically have omega-3 fatty acids EPA and DHA integrated as part of the phospholipid molecule. The phosphate group can be modified with simple organic molecules such as choline, ethanolamine or serine.

<span class="mw-page-title-main">Sphingomyelin</span>

Sphingomyelin is a type of sphingolipid found in animal cell membranes, especially in the membranous myelin sheath that surrounds some nerve cell axons. It usually consists of phosphocholine and ceramide, or a phosphoethanolamine head group; therefore, sphingomyelins can also be classified as sphingophospholipids. In humans, SPH represents ~85% of all sphingolipids, and typically make up 10–20 mol % of plasma membrane lipids.

<span class="mw-page-title-main">Sphingomyelin phosphodiesterase</span> Class of enzymes

Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses.

Sphingomyelin phosphodiesterase D (EC 3.1.4.41, sphingomyelinase D) is an enzyme of the sphingomyelin phosphodiesterase family with systematic name sphingomyelin ceramide-phosphohydrolase. These enzymes catalyse the hydrolysis of sphingomyelin, resulting in the formation of ceramide 1-phosphate and choline:

Phosphorylcholine is the hydrophilic polar head group of some phospholipids, which is composed of a negatively charged phosphate bonded to a small, positively charged choline group. Phosphorylcholine is part of the platelet-activating factor; the phospholipid phosphatidylcholine and sphingomyelin, the only phospholipid of the membrane that is not built with a glycerol backbone. Treatment of cell membranes, like those of RBCs, by certain enzymes, like some phospholipase A2, renders the phosphorylcholine moiety exposed to the external aqueous phase, and thus accessible for recognition by the immune system. Antibodies against phosphorylcholine are naturally occurring autoantibodies that are created by CD5+/B-1 B cells and are referred to as non-pathogenic autoantibodies.

<span class="mw-page-title-main">Citicoline</span> Chemical compound

Citicoline (INN), also known as cytidine diphosphate-choline (CDP-Choline) or cytidine 5'-diphosphocholine is an intermediate in the generation of phosphatidylcholine from choline, a common biochemical process in cell membranes. Citicoline is naturally occurring in the cells of human and animal tissue, in particular the organs.

In enzymology, sphingosine N-acyltransferases (ceramide synthases (CerS), EC 2.3.1.24) are enzymes that catalyze the chemical reaction of synthesis of ceramide:

In enzymology, a 1-alkenyl-2-acylglycerol choline phosphotransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">CDP-diacylglycerol—inositol 3-phosphatidyltransferase</span>

In enzymology, a CDP-diacylglycerol—inositol 3-phosphatidyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a CDP-diacylglycerol—serine O-phosphatidyltransferase is an enzyme that catalyzes the chemical reaction

Choline-phosphate cytidylyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Diacylglycerol cholinephosphotransferase</span>

In enzymology, a diacylglycerol cholinephosphotransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an ethanolaminephosphotransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidylcholine synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a sphingomyelin synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a sphingosine cholinephosphotransferase is an enzyme that catalyzes the chemical reaction

Sphingomyelin deacylase (EC 3.5.1.109, SM deacylase, GcSM deacylase, glucosylceramide sphingomyelin deacylase, sphingomyelin glucosylceramide deacylase, SM glucosylceramide GCer deacylase, SM-GCer deacylase, SMGCer deacylase) is an enzyme with systematic name N-acyl-sphingosylphosphorylcholine amidohydrolase. This enzyme catalyses the following chemical reaction

Acid sphingomyelinase is one of the enzymes that make up the sphingomyelinase (SMase) family, responsible for catalyzing the breakdown of sphingomyelin to ceramide and phosphorylcholine. They are organized into alkaline, neutral, and acidic SMase depending on the pH in which their enzymatic activity is optimal. Acid Sphingomyelinases (aSMases) enzymatic activity can be influenced by drugs, lipids, cations, pH, redox and other proteins in the environment. Specifically aSMases have been shown to have increased enzymatic activity in lysobisphosphatidic acid (LBPA) or phosphatidylinositol (PI) enriched environments, and inhibited activity when phosphorylated derivatives of PI are present.

In enzymology, a ceramide phosphoethanolamine synthase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">CDP-choline pathway</span>

The CDP-choline pathway, first identified by Eugene P. Kennedy in 1956, is the predominant mechanism by which mammalian cells synthesize phosphatidylcholine (PC) for incorporation into membranes or lipid-derived signalling molecules. The CDP-choline pathway represents one half of what is known as the Kennedy pathway. The other half is the CDP-ethanolamine pathway which is responsible for the biosynthesis of the phospholipid phosphatidylethanolamine (PE).

References