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Leukotriene C(4) synthase.

Bing K Lam1

  • 1Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115, USA. blam@rics.bwh.harvard.edu

Prostaglandins, Leukotrienes, and Essential Fatty Acids
|August 5, 2003
PubMed
Summary
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LTC(4) synthase, crucial for cysteinyl leukotriene production, is a membrane protein whose activity is modulated by metal ions. Its gene lacks TATA elements, impacting inflammatory responses in mice.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Leukotriene C4 (LTC4) synthase catalyzes the conjugation of Leukotriene A4 (LTA4) with glutathione (GSH), forming LTC4, the primary cysteinyl leukotriene.
  • LTC4 synthase is a membrane-bound homodimer, with enzymatic activity influenced by divalent cations like Mg(2+) and Co(2+).

Purpose of the Study:

  • To characterize the biochemical properties and structural homology of LTC4 synthase.
  • To investigate the roles of specific amino acid residues in LTC4 synthase catalysis.
  • To explore the transcriptional regulation and in vivo function of the LTC4 synthase gene.

Main Methods:

  • Enzyme kinetics assays were performed to determine kinetic parameters (Km, Vmax) for LTA4 and GSH.
  • Sequence and secondary structure homology analysis was conducted comparing LTC4 synthase to related proteins (FLAP, mGST-2, mGST-3).

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  • Site-directed mutagenesis was used to probe the function of key amino acid residues (Arg-51, Tyr-93).
  • Analysis of LTC4 synthase gene transcription and phenotypic assessment of gene-disrupted mice.

    • Main Results:

    • Human LTC4 synthase exhibits specific kinetic parameters for LTA4 and GSH.
    • Significant homology was observed between LTC4 synthase and FLAP, mGST-2, and mGST-3.
    • Arg-51 and Tyr-93 were identified as critical residues for epoxide ring opening and GSH thiolate anion formation, respectively.
    • The LTC4 synthase gene is TATA-less, regulated by various elements, and its disruption in mice leads to normal growth but attenuated inflammatory responses.

    Conclusions:

    • LTC4 synthase is a key enzyme in leukotriene biosynthesis with conserved structural features.
    • Specific amino acid residues play crucial roles in the catalytic mechanism of LTC4 synthase.
    • The transcriptional regulation and in vivo function of LTC4 synthase impact inflammatory pathways.