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Literature summary extracted from

  • Lansmann, S.; Ferlinz, K.; Hurwitz, R.; Bartelsen, O.; Glombitza, G.; Sandhoff, K.
    Purification of acid sphingomyelinase from human placenta: Characterization and N-terminal sequence (1996), FEBS Lett., 399, 227-231.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.12 0.025
-
sphingomyelin
-
Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.12 60000
-
x * 75000 with SDS-PAGE and western blotting analysis, x * 60000 than deglycosylated Homo sapiens
3.1.4.12 75000
-
x * 75000 with SDS-PAGE and western blotting analysis, x * 60000 than deglycosylated Homo sapiens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.12 110000fold Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.12 placenta
-
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
-
different assay conditions, substrates etc. Homo sapiens

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.1.4.12 ? x * 75000 with SDS-PAGE and western blotting analysis, x * 60000 than deglycosylated Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.12 4.6 4.7
-
Homo sapiens