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Literature summary for 3.1.4.12 extracted from

  • Sogabe, T.; Ota, H.; Iwasaki, M.; Sakasegawa, S.; Tamura, T.
    Sphingomyelinase C from Streptomyces sp. A9107: unusual primary structure for bacterial sphingomyelinase C (2012), J. Biosci. Bioeng., 114, 398-401.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
functional overexpression in Rhodococcus erythropolis and secretion to the culture medium Streptomyces sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Streptomyces sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ slightly activates, Km is 1.40 mM Streptomyces sp.
Co2+ activates, Km is 1.46 mM Streptomyces sp.
Mg2+ activates, Km is 1.29 mM Streptomyces sp.
Mn2+ activates, most effective divalent metal ion, Km is 0.94 mM Streptomyces sp.
additional information central metal-binding site residues N77, E119, D265, N267, D374, and H375 are completely conserved in the enzyme Streptomyces sp.
Sr2+ slightly activates, Km is 2.42 mM Streptomyces sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion Streptomyces sp.
37000
-
gel filtration Streptomyces sp.
41540
-
1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion Streptomyces sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a sphingomyelin + H2O Streptomyces sp.
-
a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?
a sphingomyelin + H2O Streptomyces sp. A9107
-
a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?

Organism

Organism UniProt Comment Textmining
Streptomyces sp. I4DXK5
-
-
Streptomyces sp. A9107 I4DXK5
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a sphingomyelin + H2O
-
Streptomyces sp. a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?
a sphingomyelin + H2O
-
Streptomyces sp. A9107 a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?
additional information substrate specificity, the enzyme is highly sphingomyelin-specific, it may not have sphingomyelinase D activity, because it does not hydrolyze the ester linkage between ceramide phosphate and choline. Of the phospholipids tested, the enzyme hydrolyzes only the ester linkage between ceramide and phosphocholine and has no activity toward phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylinositol Streptomyces sp. ?
-
?
additional information substrate specificity, the enzyme is highly sphingomyelin-specific, it may not have sphingomyelinase D activity, because it does not hydrolyze the ester linkage between ceramide phosphate and choline. Of the phospholipids tested, the enzyme hydrolyzes only the ester linkage between ceramide and phosphocholine and has no activity toward phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylinositol Streptomyces sp. A9107 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion Streptomyces sp.

Synonyms

Synonyms Comment Organism
S-SMase
-
Streptomyces sp.
SMase
-
Streptomyces sp.
sphingomyelinase C
-
Streptomyces sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Streptomyces sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Streptomyces sp.

General Information

General Information Comment Organism
evolution the enzyme from Streptomyces seems to be a typical bacterial SMase with a primary structure unusual for known bacterial SMases, primary structure comparisons and phylogenetic analysis Streptomyces sp.