Catalytic Mechanism of Eukaryotic Neutral Ceramidase

Lucy Malinina, Rhoderick E Brown

Research output: Contribution to journalShort surveypeer-review

2 Scopus citations

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.

Original languageEnglish (US)
Article number3236
Pages (from-to)1371-1372
Number of pages2
JournalStructure
Volume23
Issue number8
DOIs
StatePublished - Aug 7 2015

Fingerprint Dive into the research topics of 'Catalytic Mechanism of Eukaryotic Neutral Ceramidase'. Together they form a unique fingerprint.

Cite this