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Literature summary extracted from

  • Obama, T.; Kan, Y.; Ikezawa, H.; Imagawa, M.; Tsukamoto, K.
    Glu-53 of Bacillus cereus sphingomyelinase acts as an indispensable ligand of Mg2+ essential for catalytic activity (2003), J. Biochem., 133, 279-286.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.12 expression in Bacillus brevis Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.12 E53A no sphingomyelin hydrolyzing and no hemolytic activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity Bacillus cereus
3.1.4.12 E53D 5% of wild-type sphingomyelin hydrolyzing activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity Bacillus cereus
3.1.4.12 E53Q no sphingomyelin hydrolyzing and no hemolytic activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.12 Ca2+ 6.9 mM, 50% inhibitiion Bacillus cereus
3.1.4.12 Cu2+ 0.0079 mM, 50% inhibitiion Bacillus cereus
3.1.4.12 Zn2+ 0.0042 mM, 50% inhibitiion, higher concentrations of Mg2+ slighty restore activity Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.12 0.35
-
 sphingomyelin 37°C, pH 7.5 Bacillus cereus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.12 extracellular
-
 Bacillus cereus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.12 Co2+ can replace Mg2+, 50% activation at 0.0015 mM Bacillus cereus
3.1.4.12 Mg2+ two-step activation, high-affinity binding site with 50% saturation at 0.0041 mM, low-affinity-binding site with 50% saturation at 20 mM, approx. 5fold activation at 20 mM Bacillus cereus
3.1.4.12 Mn2+ can replace Mg2+, 50% activation at 0.00087 mM Bacillus cereus

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 Bacillus cereus
-
 N-acylsphingosine + choline phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Bacillus cereus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.12 recombinant SMase Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.12 2-hexadecanoylamino-4-nitrophenylphosphocholine + H2O
-
 Bacillus cereus 2-hexadecanoylamino-4-nitrophenol + choline phosphate
-
 ?
3.1.4.12 lysophosphatidylcholine + H2O
-
 Bacillus cereus acylglycerol + choline phosphate
-
 ?
3.1.4.12 sphingomyelin + H2O
-
 Bacillus cereus N-acylsphingosine + choline phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 SMase
-
 Bacillus cereus
3.1.4.12 sphingomyelinase
-
 Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.4.12 5.9
-
 2-hexadecanoylamino-4-nitrophenylphosphocholine 37°C, pH 7.5 Bacillus cereus
3.1.4.12 13
-
 lysophosphatidylcholine 37°C, pH 7.5 Bacillus cereus
3.1.4.12 210
-
 sphingomyelin 37°C, pH 7.5 Bacillus cereus