What is the function of sphingomyelinase?

What is the function of sphingomyelinase?

Introduction: Sphingomyelinases, which catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine, are abundant in the brain. These enzymes are a major, rapid source of ceramide production not only during physiological responses to receptor stimulation, but also in neurological disorders.

How does acid sphingomyelinase work?

The enzyme acid sphingomyelinase catalyzes the hydrolysis of sphingomyelin to ceramide. The importance of the enzyme for cell functions was first recognized in Niemann-Pick disease type A and B, the genetic disorders with a massive accumulation of sphingomyelin in many organs.

Which class of enzymes does sphingomyelinase belong to?

Sphingomyelinase D (SMase D), isolated from Loxosceles laeta, catalyses the hydrolysis of sphingomyelin to ceramide 1-phosphate (C1P) and choline, and the hydrolysis of lysophosphatidyl choline to lysophosphatidic acid (LPA) and choline. This enzyme belongs to class I of the SMase D enzymes.

Where is the SMPD1 gene located?

The SMPD1 gene provides instructions for making an enzyme called acid sphingomyelinase. This enzyme is found in lysosomes, which are small compartments in the cell that digest and recycle molecules.

What is the substrate for acid sphingomyelinase?

The acid sphingomyelinase (ASM) activity is dependent on Zn2+ which requires exogenous Zn2+ ions in the assay to retain full activity while L-ASM does not need additional Zn2+ ions in the assay buffer because Zn2+ tightly binds to the enzyme.

What is structure of sphingosine?

C18H37NO2
Sphingosine/Formula

What is sphingomyelinase deficiency?

Sphingomyelinase deficiency: Also called Niemann-Pick disease, this is a disorder of the metabolism of a lipid (fat) called sphingomyelin that usually causes the progressive development of enlargement of the liver and spleen (hepatosplenomegaly), “swollen glands” (lymphadenopathy), anemia and mental and physical …

How is ASMD diagnosed?

A diagnosis of ASMD is based upon identification of characteristic symptoms, a detailed patient history, a thorough clinical evaluation and a variety of specialized tests. Individuals suspected of ASMD will be tested to determine whether the activity of the enzyme, ASM, is reduced or absent.

What kind of enzyme is acid sphingomyelinase 1?

Sphingomyelin phosphodiesterase 1 (SMPD1), also known as acid sphingomyelinase (ASM), is an enzyme that in humans is encoded by the SMPD1 gene.

What is the role of neutral Sphingomyelin phosphodiesterase?

Sphingomyelin phosphodiesterase (EC 3.1.4.12, also known as neutral sphingomyelinase, sphingomyelinase, or SMase) 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.

Which is responsible for the production of sphingomyelin?

Sphingomyelin synthase is responsible for the production of sphingomyelin from ceramide. Diacylglycerol is produced as a byproduct when the phosphocholine is transferred. Sphingomyelin breakdown is responsible for initiating many universal signaling pathways.

What causes the accumulation of sphingomyelin in the brain?

It is a genetically-inherited disease caused by a deficiency in the lysosomal enzyme acid sphingomyelinase, which causes the accumulation of sphingomyelin in spleen, liver, lungs, bone marrow, and brain, causing irreversible neurological damage. Of the two types involving sphingomyelinase, type A occurs in infants.