A novel brain-expressed protein related to carnitine palmitoyltransferase I

NT Price*, FR van der Leij, VN Jackson, CG Corstorphine, R Thomson, A Sorensen, VA Zammit

*Corresponding author for this work

    Research output: Contribution to journalArticleAcademicpeer-review

    187 Citations (Scopus)

    Abstract

    Malonyl-CoenzymeA acts as a fuel sensor, being both an intermediate of fatty acid synthesis and an inhibitor of the two known isoforms of carnitine palmitoyltransferase I (CPT I), which control mitochondrial fatty acid oxidation. We describe here a novel CPT1 family member whose mRNA is present predominantly in brain and testis. Chromosomal locations and genome organization are reported for the mouse and human genes. The protein sequence contains all the residues known to be important for both carnitine acyltransferase activity and malonyl-CoA binding in other family members. Yeast expressed protein has no detectable catalytic activity with several different acyl-CoA esters that are good substrates for other carnitine acyltransferases, including the liver isoform of CPT I, which is also expressed in brain; however, it displays high-affinity malonyl-CoA binding. Thus this new CPT I related protein may be specialized for the metabolism of a distinct class of fatty acids involved in brain function.

    Original languageEnglish
    Pages (from-to)433-442
    Number of pages10
    JournalGENOMICS
    Volume80
    Issue number4
    DOIs
    Publication statusPublished - Oct-2002

    Keywords

    • carnitine palmitoyltransferase I
    • brain
    • malonyl-CoA
    • SITE-DIRECTED MUTAGENESIS
    • 2 HISTIDINE-RESIDUES
    • N-TERMINAL DOMAIN
    • RAT-LIVER
    • MALONYL-COA
    • CPT-I
    • FATTY-ACID
    • CATALYTIC ACTIVITY
    • MOLECULAR ANALYSIS
    • ENERGY-BALANCE

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