Development of an acid ceramidase activity-based probe

Cécile M J Ouairy; Maria J Ferraz; Rolf G Boot; Marc P Baggelaar; Mario van der Stelt; Monique Appelman; Gijsbert A van der Marel; Bogdan I Florea; Johannes M F G Aerts; Herman S Overkleeft

doi:10.1039/c5cc00356c

Development of an acid ceramidase activity-based probe

Cécile M J Ouairy, Maria J Ferraz, Rolf G Boot, Marc P Baggelaar, Mario van der Stelt, Monique Appelman, Gijsbert A van der Marel, Bogdan I Florea, Johannes M F G Aerts, Herman S Overkleeft

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Acid ceramidase is responsible for the ultimate step in the catabolism of (glyco)sphingolipids by hydrolysis of ceramide into sphingosine and free fatty acid. Deficiency in acid ceramidase is the molecular basis of Farber disease. Here we report the synthesis and characterization of an activity-based acid ceramidase probe.

Original language	English
Pages (from-to)	6161-3
Number of pages	3
Journal	Chemical communications (Cambridge, England)
Volume	51
Issue number	28
DOIs	https://doi.org/10.1039/c5cc00356c
Publication status	Published - 11 Apr 2015
Externally published	Yes

Keywords

Acid Ceramidase/analysis
Ceramides/chemistry
Enzyme Activation
Fatty Acids/chemistry
Hydrolysis
Molecular Probes/chemical synthesis
Molecular Structure
Sphingolipids/chemistry
Sphingosine/chemistry

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10.1039/c5cc00356c

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title = "Development of an acid ceramidase activity-based probe",

abstract = "Acid ceramidase is responsible for the ultimate step in the catabolism of (glyco)sphingolipids by hydrolysis of ceramide into sphingosine and free fatty acid. Deficiency in acid ceramidase is the molecular basis of Farber disease. Here we report the synthesis and characterization of an activity-based acid ceramidase probe.",

keywords = "Acid Ceramidase/analysis, Ceramides/chemistry, Enzyme Activation, Fatty Acids/chemistry, Hydrolysis, Molecular Probes/chemical synthesis, Molecular Structure, Sphingolipids/chemistry, Sphingosine/chemistry",

author = "Ouairy, {C{\'e}cile M J} and Ferraz, {Maria J} and Boot, {Rolf G} and Baggelaar, {Marc P} and {van der Stelt}, Mario and Monique Appelman and {van der Marel}, {Gijsbert A} and Florea, {Bogdan I} and Aerts, {Johannes M F G} and Overkleeft, {Herman S}",

year = "2015",

month = apr,

day = "11",

doi = "10.1039/c5cc00356c",

language = "English",

volume = "51",

pages = "6161--3",

journal = "Chemical communications (Cambridge, England)",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "28",

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TY - JOUR

T1 - Development of an acid ceramidase activity-based probe

AU - Ouairy, Cécile M J

AU - Ferraz, Maria J

AU - Boot, Rolf G

AU - Baggelaar, Marc P

AU - van der Stelt, Mario

AU - Appelman, Monique

AU - van der Marel, Gijsbert A

AU - Florea, Bogdan I

AU - Aerts, Johannes M F G

AU - Overkleeft, Herman S

PY - 2015/4/11

Y1 - 2015/4/11

N2 - Acid ceramidase is responsible for the ultimate step in the catabolism of (glyco)sphingolipids by hydrolysis of ceramide into sphingosine and free fatty acid. Deficiency in acid ceramidase is the molecular basis of Farber disease. Here we report the synthesis and characterization of an activity-based acid ceramidase probe.

AB - Acid ceramidase is responsible for the ultimate step in the catabolism of (glyco)sphingolipids by hydrolysis of ceramide into sphingosine and free fatty acid. Deficiency in acid ceramidase is the molecular basis of Farber disease. Here we report the synthesis and characterization of an activity-based acid ceramidase probe.

KW - Acid Ceramidase/analysis

KW - Ceramides/chemistry

KW - Enzyme Activation

KW - Fatty Acids/chemistry

KW - Hydrolysis

KW - Molecular Probes/chemical synthesis

KW - Molecular Structure

KW - Sphingolipids/chemistry

KW - Sphingosine/chemistry

U2 - 10.1039/c5cc00356c

DO - 10.1039/c5cc00356c

M3 - Article

C2 - 25748248

SN - 1359-7345

VL - 51

SP - 6161

EP - 6163

JO - Chemical communications (Cambridge, England)

JF - Chemical communications (Cambridge, England)

IS - 28

ER -

Development of an acid ceramidase activity-based probe

Abstract

Keywords

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