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Literature summary extracted from

  • Perrotta, C.; Clementi, E.
    Biological roles of Acid and neutral sphingomyelinases and their regulation by nitric oxide (2010), Physiology, 25, 64-71.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.12 lysosome lysosomal phosphodiesterase acid SMase Homo sapiens 5764
-
3.1.4.12 plasma membrane membrane-bound neutral SMase Homo sapiens 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.12 Mg2+ required by N-SMase Homo sapiens
3.1.4.12 Zn2+ required by the secreted enzyme form Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.12 70000
-
x * 71000, N-SMase2, SDS-PAGE, x * 70000, mature A-SMase, SDS-PAGE, x * 75000, pre-pro-form of A-SMase, SDS-PAGE Homo sapiens
3.1.4.12 71000
-
x * 71000, N-SMase2, SDS-PAGE, x * 70000, mature A-SMase, SDS-PAGE, x * 75000, pre-pro-form of A-SMase, SDS-PAGE Homo sapiens
3.1.4.12 75000
-
x * 71000, N-SMase2, SDS-PAGE, x * 70000, mature A-SMase, SDS-PAGE, x * 75000, pre-pro-form of A-SMase, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.12 a sphingomyelin + H2O Homo sapiens
-
a ceramide + choline phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.12 glycoprotein the mature form and its precursors have six potential N-glycosylation sites, and at least five of them are important for proper folding, protection against proteolysis, and enzymatic activity of A-SMase. A-SMase has a mannose 6-phosphate residue that is required for lysosomal targetting of the enzyme via the mannose 6-phosphate receptor Homo sapiens
3.1.4.12 proteolytic modification the 75-kDa pre-proform of A-SMase, which is a pre-polypeptide with little if any enzymatic activity in the endoplasmic reticulum, is cleaved to an intermediate pro-form of 72 kDa, and further to the mature enzyme of 70 kDa in the lysosomes Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.12 astrocyte cortical astrocyte, acid SMase Homo sapiens
-
3.1.4.12 brain brain-specific N-SMase2 Homo sapiens
-
3.1.4.12 microglia acid SMase Homo sapiens
-
3.1.4.12 T-lymphocyte
-
Homo sapiens
-
3.1.4.12 U-937 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.12 a sphingomyelin + H2O
-
Homo sapiens a ceramide + choline phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.4.12 ? x * 71000, N-SMase2, SDS-PAGE, x * 70000, mature A-SMase, SDS-PAGE, x * 75000, pre-pro-form of A-SMase, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 A-SMase
-
Homo sapiens
3.1.4.12 acid SMase
-
Homo sapiens
3.1.4.12 acid sphingomyelinase
-
Homo sapiens
3.1.4.12 N-SMase
-
Homo sapiens
3.1.4.12 neutral SMase
-
Homo sapiens
3.1.4.12 neutral sphingomyelinase
-
Homo sapiens

General Information

EC Number General Information Comment Organism
3.1.4.12 malfunction deficiency of the enzyme leads to lysosomal accumulation of sphingomyelin resulting in in Niemann-Pick types A and B diseases Homo sapiens
3.1.4.12 metabolism interaction in the NO/NOS and SMases/ceramide signaling pathways, overview Homo sapiens
3.1.4.12 additional information from the gene of A-SMase, another product may be generated, i.e., the secretory SMase, which is very similar to A-SMase, differing only in the intracellular trafficking and in the need of zinc for activation Homo sapiens
3.1.4.12 physiological function role for A-SMase in the release of plasma membrane-derived microparticles, overview A-SMase is a cation-independent hydrolase contributing to the catabolism of sphingomyelin in lysosomes. Stress is believed to activate A-SMase to generate ceramide, which serves as a cellular mediator in initiating apoptotic response, the process is controlled by NO, detailed overview. A-SMase activity is also crucial for developmental programmed cell death of oocytes. Modeling of A-SMase function in apoptosis, overview Homo sapiens