Sandbox Reserved 313
This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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2dds, resolution 1.80Å () | |||||||||
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Activity: | Sphingomyelin phosphodiesterase, with EC number 3.1.4.12 | ||||||||
Related: | 2ddr, 2ddt | ||||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
IntroductionIntroduction
Sphingomyelin phosphodiesterase (SMase) is an enzyme which catalyzes the hydrolysis of sphingomyelin to ceramide and phosphocholine [1]. There are 6 known types of sphingomyelinases:
Acid sphingomyelinase (aSMase) -
Secretory sphingomyelinase (sSMase) -
Neutral, Mg2+-dependent sphingomyelinases (nSMase) -
Mg2+-independent neutral sphingomyelinases -
Alkaline sphingomyelinase -
Bacterial sphingomyelinase -
Structure and FunctionStructure and Function
MechanismMechanism
Importance of SMaseImportance of SMase
ReferencesReferences
- ↑ Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J. Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus. J Biol Chem. 2006 Jun 9;281(23):16157-67. Epub 2006 Apr 4. PMID:16595670 doi:10.1074/jbc.M601089200