title: Catalytic Mechanism of Eukaryotic Neutral Ceramidase.
abstract: Neutral ceramidases are key enzymes of sphingolipid metabolism that hydrolyze the fatty acyl/sphingosine amide linkage of ceramide at neutral pH. In this issue of Structure, Airola et al. (2015) present the first crystal structure of human nCDase and show how complexation with phosphate supports a new catalytic mechanism for Zn-dependent amidases while providing a structurally based explanation for ceramide specificity.
authors.affiliation: Hormel Institute, University of Minnesota, Austin, MN 55912, USA. Electronic address: lucy@hi.umn.edu.
authors.forename: Lucy
authors.initials: L
authors.lastname: Malinina
authors.affiliation: Hormel Institute, University of Minnesota, Austin, MN 55912, USA. Electronic address: reb@umn.edu.
authors.forename: Rhoderick E
authors.initials: RE
authors.lastname: Brown
mesh_terms: D000818:Animals; D002518:Ceramides / Q000737:chemistry*; D006801:Humans; D008246:Lysophospholipids / Q000737:chemistry*; D055576:Neutral Ceramidase / Q000737:chemistry*; D013110:Sphingosine / Q000031:analogs & derivatives* / Q000737:chemistry*
chemical_list: D002518:Ceramides; D008246:Lysophospholipids; D055576:Neutral Ceramidase; D013110:Sphingosine