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Selenocysteine Lyase: Mechanism, Structure, and Biological Role

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Abstract

Selenocysteine lyase is a homodimeric pyridoxal 5′-phosphate-dependent enzyme that specifically catalyzes the removal of selenium from l-selenocysteine to yield l-alanine and is inert to its cognate l-cysteine. The enzyme is proposed to function in the recycling of the micronutrient selenium from degraded selenoproteins that contain selenocysteine residues as an essential component. Findings from recent studies have facilitated an unprecedented understanding of how this unique enzyme distinguishes between selenocysteine and cysteine and have suggested possible directions for future research that may uncover the physiological role of the enzyme in mammals.

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Author information

Authors and Affiliations

  1. Department of Biotechnology, Institute of Science and Engineering, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan

    Hisaaki Mihara

  2. Institute for Chemical Research, Kyoto University, Uji, Kyoto, 611-0011, Japan

    Nobuyoshi Esaki

Authors
  1. Hisaaki Mihara
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  2. Nobuyoshi Esaki
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Corresponding author

Correspondence to Hisaaki Mihara .

Editor information

Editors and Affiliations

  1. National Cancer Institute, Basic Research Laboratory, National Institutes of Health, Bethesda, 20892, Maryland, USA

    Dolph L. Hatfield

  2. University of Hawaii, Monoa, Dole Street 2444, Honolulu, 96822, Hawaii, USA

    Marla J. Berry

  3. , Division of Genetics, Department of Medi, Brigham and Women’s Hospital and Harvard, Avenue Louis Pasteur 77, Boston, 02115, USA

    Vadim N. Gladyshev

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© 2011 Springer Science+Business Media, LLC

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Mihara, H., Esaki, N. (2011). Selenocysteine Lyase: Mechanism, Structure, and Biological Role. In: Hatfield, D., Berry, M., Gladyshev, V. (eds) Selenium. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1025-6_8

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