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Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine.

Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine. Research Abstract Details 

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  • Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine. Abstract Text:

    sujoy lahiriSujoy Lahiri,hyunmi leeHyunmi Lee,judith mesicekJudith Mesicek,zvi fuksZvi Fuks,adriana haimovitz-friedmanAdriana Haimovitz-Friedman,richard n kolesnickRichard N Kolesnick,anthony h futermanAnthony H Futerman,sujoy lahiriSujoy Lahiri,hyunmi leeHyunmi Lee,judith mesicekJudith Mesicek,zvi fuksZvi Fuks,adriana haimovitz-friedmanAdriana Haimovitz-Friedman,richard n kolesnickRichard N Kolesnick,anthony h futermanAnthony H Futerman,sujoy lahiriSujoy Lahiri,hyunmi leeHyunmi Lee,judith mesicekJudith Mesicek,zvi fuksZvi Fuks,adriana haimovitz-friedmanAdriana Haimovitz-Friedman,richard n kolesnickRichard N Kolesnick,anthony h futermanAnthony H Futerman,

    Ceramide is a key metabolite in the pathway of sphingolipid biosynthesis. In mammals, ceramide is synthesized by N-acylation of a sphingoid long-chain base by a family of ceramide synthases (CerS), each of which displays a high specificity towards acyl CoAs of different chain lengths. We now optimize a previously-described assay for measuring CerS activity for use upon over-expression of mammalian CerS, and using these conditions, establish the K(m) value of each CerS towards sphinganine. Remarkably, the K(m) values towards sphinganine are all similar, ranging from 2 to 5muM, even for CerS proteins that are able to use more than one acyl CoA for ceramide synthesis (i.e. CerS4). The availability of this assay will permit further accurate characterization of the kinetic parameters of mammalian CerS proteins.

    Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine. Publishing Authors By Initials

    s lahiriS Lahiri,h leeH Lee,j mesicekJ Mesicek,z fuksZ Fuks,a haimovitz-friedmanA Haimovitz-Friedman,rn kolesnickRN Kolesnick,ah futermanAH Futerman,s lahiriS Lahiri,h leeH Lee,j mesicekJ Mesicek,z fuksZ Fuks,a haimovitz-friedmanA Haimovitz-Friedman,rn kolesnickRN Kolesnick,ah futermanAH Futerman,s lahiriS Lahiri,h leeH Lee,j mesicekJ Mesicek,z fuksZ Fuks,a haimovitz-friedmanA Haimovitz-Friedman,rn kolesnickRN Kolesnick,ah futermanAH Futerman,

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    Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: FEBS letters

    VOLUME: 581

    Page Numbers: 5289-94

    Journal Abbreviation: FEBS Lett.

    ISSN: 0014-5793

    DAY: 23

    MONTH: 10

    YEAR: 2007

    Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine. Information

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    LANGUAGE: eng

    NlmUniqueID: 155157

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    Grant and Affiliation Information for Kinetic characterization of mammalian ceramide synthases: Determination of K(m) values towards sphinganine.

    AFFILIATION: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

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    MEDLINETA: FEBS Lett

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