Catalytic Mechanism of Eukaryotic Neutral Ceramidase

Lucy Malinina; Rhoderick E Brown

doi:10.1016/j.str.2015.07.003

Catalytic Mechanism of Eukaryotic Neutral Ceramidase

Lucy Malinina, Rhoderick E Brown

The Hormel Institute

Research output: Contribution to journal › Short survey › peer-review

4 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 language	English (US)
Article number	3236
Pages (from-to)	1371-1372
Number of pages	2
Journal	Structure
Volume	23
Issue number	8
DOIs	https://doi.org/10.1016/j.str.2015.07.003
State	Published - Aug 7 2015

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© 2015 Elsevier Ltd.

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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.",

author = "Lucy Malinina and Brown, {Rhoderick E}",

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Catalytic Mechanism of Eukaryotic Neutral Ceramidase

Abstract

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