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Literature summary extracted from

  • Gorelik, A.; Illes, K.; Heinz, L.X.; Superti-Furga, G.; Nagar, B.
    Crystal structure of mammalian acid sphingomyelinase (2016), Nat. Commun., 7, 12196 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.12 expressed in Sf9 cells Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.12 sitting drop vapor diffusion method, using 0.2M lithium acetate and 20% (w/v) PEG 3350 Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.12 F388R the mutant shows reduced activity with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme Mus musculus
3.1.4.12 H280A inactive with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate Mus musculus
3.1.4.12 H317A inactive with sphingomyelin as substrate, but active with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme Mus musculus
3.1.4.12 L391R the mutant shows about 20% activity with sphingomyelin and about 50% activity with bis(4-nitrophenyl)phosphate as substrate, as compared to the wild type enzyme Mus musculus
3.1.4.12 P321E the mutant shows reduced activity with sphingomyelin and almost no activity with bis(4-nitrophenyl)phosphate as substrate, compared to the wild type enzyme Mus musculus
3.1.4.12 V128E the mutant shows about 20% activity with sphingomyelin and about 70% activity with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme Mus musculus
3.1.4.12 V143R the mutant shows about 5% activity with sphingomyelin and about 65% activity with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme Mus musculus
3.1.4.12 W283N the mutant shows reduced activity with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.12 1-aminodecylidene bis-phosphonic acid
-
 Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.12 lysosome
-
 Mus musculus 5764
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.12 Zn2+ contains two zinc ions Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.12 sphingomyelin + H2O Mus musculus
-
 ceramide + phosphocholine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Mus musculus Q04519
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.12 glycoprotein the protein has five sites of N-glycosylation Mus musculus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.12 Ni-NTA resin column chromatography and Superdex 200 gel filtration Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.12 bis(4-nitrophenyl)phosphate + H2O
-
 Mus musculus ?
-
 ?
3.1.4.12 sphingomyelin + H2O
-
 Mus musculus ceramide + phosphocholine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.12 ? x * 60000, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 acid sphingomyelinase
-
 Mus musculus
3.1.4.12 ASM
-
 Mus musculus
3.1.4.12 aSMase
-
 Mus musculus
3.1.4.12 SMPD1
-
 Mus musculus

General Information

EC Number General Information Comment Organism
3.1.4.12 malfunction inactivating enzyme mutations cause Niemann-Pick disease Mus musculus