Structure and Function of Δ9-Fatty Acid Desaturase

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Author(s)

Abstract

<p>Δ9-Fatty acid desaturase (Δ9-desaturase) is a rate-limiting enzyme of unsaturated fatty acid biosynthesis in animal cells and specifically introduces a <i>cis</i>-double bond at the Δ9-position of acyl-CoA. Since the chemical structure of fatty acids determines the physicochemical properties of cellular membrane and modulates a broad range of cellular functions, double bond introduction into a fatty acid by Δ9-desaturase should be specifically carried out. Reported crystal structures of stearoyl-CoA desaturase (SCD)1, one of the most studied Δ9-desaturases, have revealed the mechanism underlying the determination of substrate preference, as well as the position (Δ9) and conformation (<i>cis</i>) of double bond introduction. The crystal structures of SCD1 have also provided insights into the function of other Δ9-desaturases, including <i>Drosophila</i> homologs. Moreover, the amino-terminal sequences of Δ9-desaturases are shown to have unique roles in protein degradation. In this review, we introduce recent advances in the understanding of the function and regulation of Δ9-desaturase from the standpoint of protein structure.</p>

Journal

  • Chemical and Pharmaceutical Bulletin

    Chemical and Pharmaceutical Bulletin 67(4), 327-332, 2019

    The Pharmaceutical Society of Japan

Codes

  • NII Article ID (NAID)
    130007621738
  • NII NACSIS-CAT ID (NCID)
    AA00602100
  • Text Lang
    ENG
  • ISSN
    0009-2363
  • NDL Article ID
    029604355
  • NDL Call No.
    Z53-D167
  • Data Source
    NDL  J-STAGE 
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