Sphingomyelinase

spinqualitylabelsall models Sphingomyelinase complex with glycerol and phosphate ion (PDB entry [[21zwx]) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Sphingomyelinase (SMase) or sphingomyelin phosphodiesterase is a hydrolase involved in sphingolipid metabolism. It catalyzes the breakdown of sphingomyelin (SM) to phosphocholine and ceramide. The SMase is classified into 5 types according to their pH dependence and cation dependence. Acid SMase-like phosphodiesterase is a paralog of acid SMase and thus though related by gene duplication has different functions. Acid SMase-like phosphodiesterase 3A hydrolyzes nucleotides triphosphates and diphosphates while Acid SMase-like phosphodiesterase 3B is a GPI-anchored protein with role in inflammatory processes and kidney disease. Disease Mutations in acid SMase are found in patients with Niemann-Pick disease.

3D structures of sphingomyelinase

Updated on 09-November-2020

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• SMase
  • 5uvg – hSMase catalytic domain – human
    
  • 3rlh, 3rlg – SMase D (mutant) – Loxosceles intermedia
    
  • 1xx1, 2f9r – SMase I – Loxosceles laeta
    
  • 1zwx – SMase C – Listeria ivanovii
    
  • 2ddr, 2dds, 2ddt – BcSMase + cation – Bacillus cereus
    
  • 2uyr – BcSMase (mutant)
    
  • 7cne – SMase C – Streptomyces griseocarneus
    
• Acid SMase
  • 5jg8, 5i81, 5i8r – hSMase
    
  • 5i85 – hSMase + phosphocholine
    
  • 5fib – mSMase – mouse
    
  • 5hqn – mSMase catalytic domain
    
  • 5fi9 – mSMase + inhibitor
    
  • 5fic – mSMase + lipid
    
• Acid SMase-like phosphodiesterase
  • 5ebb – hSMase 3A
    
  • 5ebe – hSMase 3A + CMP
    
  • 5fc1, 5fc7, 5fca – mSMase 3A
    
  • 5fcb – mSMase 3A + AMP
    
  • 5fc6 – mSMase 3A + AMPCP
    
  • 5fc5 – mSMase 3A + phosphocholine
    
  • 5kar – mSMase 3B
    
  • 5kas – mSMase 3B + phosphocholine
    
• Alkaline SMase
  • 5udy – hSMase
    
  • 5tcd – hSMase + phosphocholine
    

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Michal Harel, Alexander Berchansky, Joel L. Sussman