Selenoprotein Biosynthesis and Selenium-Specific Enzymes (特集1:若手が拓く微量元素研究の最前線) Selenoprotein Biosynthesis and Selenium-Specific Enzymes

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Author(s)

Abstract

Selenocysteine lyase (SCL) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that specifically acts on L-selenocysteine to yield L-alanine and selenium. The enzyme does not act on L-cysteine at all. We have recently found that RNAi-mediated depletion of SCL results in significant reductions in activities and protein levels of the selenoproteins glutathione peroxidase and thioredoxin reductase, suggesting an important cellular role of SCL in selenoprotein synthesis. Therefore, the strict discrimination between selenium and sulfur by SCL may be a key step in the specific seleniumdelivery pathway for selenoprotein synthesis. However, the mechanism for the discrimination between selenium and sulfur by SCL remains unclear. In this review, we describe function and mechanism of SCL involved in the biosynthesis of selenoprotein. We also discuss the catalytic properties of the SCL-related enzymes, cysteine desulfurases.

Journal

  • Biomedical Research on Trace Elements

    Biomedical Research on Trace Elements 17(4), 355-359, 2006-12-31

    Japan Society for Biomedical Research on Trace Elements

References:  20

Codes

  • NII Article ID (NAID)
    10018664330
  • NII NACSIS-CAT ID (NCID)
    AN10423256
  • Text Lang
    ENG
  • Article Type
    REV
  • ISSN
    0916717X
  • NDL Article ID
    8664426
  • NDL Source Classification
    ZS8(科学技術--医学--解剖学・生理学・生化学)
  • NDL Call No.
    Z19-3255
  • Data Source
    CJP  NDL  J-STAGE 
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