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Literature summary extracted from

  • Lee, C.Y.; Tamura, T.; Rabah, N.; Lee, D.Y.; Ruel, I.; Hafiane, A.; Iatan, I.; Nyholt, D.; Laporte, F.; Lazure, C.; Wada, I.; Krimbou, L.; Genest, J.
    Carboxyl-terminal disulfide bond of acid sphingomyelinase is critical for its secretion and enzymatic function (2007), Biochemistry, 46, 14969-14978.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.12 transient transfection of the His/V5-tagged wild-type and mutant recombinant ASM in CHO cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.12 G577A naturally occuring mutation, the mutant has severely defective enzymatic function Homo sapiens
3.1.4.12 additional information DELTAR608 is a naturally occuring deletion mutation, construction of five serial carboxyl-terminal deletion mutants N620, N590, N570, N510, and N490, none of which, except the smallest deletion mutant N620 that preserves all post-translational modifications, are found capable of secretion to the medium, only the N620 deletion mutant conserves functional integrity with 100% wild type activity, all other mutants completely loose the ability to catalyze sphingomyelin hydrolysis, mutant DELTAR608 transfected CHO cells and fibroblasts from a compound heterozygous Niemann-Pick disease type B patient, DELTAR608 and R441X, have defective translocation to the plasma membrane, deletion mutants DELTAR608 and N590 are trapped in the endoplasmic reticulum quality control checkpoint in contrast to the wild-type lysosomal localization, steady-state levels of ubiquitination are minimal for the wild-type ASM, a significant amount of Lys63-linked polyubiquitinated DELTAR608 and N590 can be purified by S5a-affinity chromatography, indicating an important misfolding in the carboxyl-terminal mutants Homo sapiens
3.1.4.12 R496L naturally occuring mutation, the mutant has severely defective enzymatic function Homo sapiens
3.1.4.12 Y537H naturally occuring mutation, the mutant has severely defective enzymatic function Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.12 extracellular ASM is a secretory protein Homo sapiens
-
-
3.1.4.12 lysosome ASM is a secretory protein Homo sapiens 5764
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.12 70000
-
 x * 70000 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 sphingomyelin + H2O Homo sapiens degradation of sphingomyelin N-acylsphingosine + choline phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Homo sapiens
-
 acid sphingomyelinase, gene SMPD-1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.12 additional information steady-state levels of ubiquitination are minimal for the wild-type ASM Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.4.12 additional information
-
 activity of wild-type and mutant enzymes, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.12 additional information structural-functional properties of its carboxyl-terminus, amino acids 462-629, the carboxyl-terminus of the ASM is crucial for its protein structure, which in turns dictates the enzymatic function and secretion, overview Homo sapiens ?
-
 ?
3.1.4.12 sphingomyelin + H2O
-
 Homo sapiens N-acylsphingosine + choline phosphate
-
 ?
3.1.4.12 sphingomyelin + H2O degradation of sphingomyelin Homo sapiens N-acylsphingosine + choline phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.12 ? x * 70000 Homo sapiens
3.1.4.12 More structural-functional properties of its carboxyl-terminus, amino acids 462-629, overview, ASM consists of a signal peptide, amino acids 1-46, in the N-terminal region, a small transmembrane domain, amino acids 25-47, a saposin B region, amino acids 87-165, that serves as an activator of various lysosomal lipid-degrading enzymes, a proline-rich region, amino acids 179-197, followed by the metallophosphoesterase catalytic domain, amino acids 199-461 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 acid sphingomyelinase
-
 Homo sapiens
3.1.4.12 ASM
-
 Homo sapiens
3.1.4.12 SMPD-1
-
 Homo sapiens
3.1.4.12 sphingomyelin phosphodiesterase 1
-
 Homo sapiens