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- Mihara Hisaaki
- Institute for Chemical Research, Kyoto University
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- Kurokawa Suguru
- Institute for Chemical Research, Kyoto University
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- Omi Rie
- Institute for Chemical Research, Kyoto University
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- Kurihara Tatsuo
- Institute for Chemical Research, Kyoto University
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- Hirotsu Ken
- Department of Chemistry, Graduate School of Science, Osaka City University
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- Esaki Nobuyoshi
- Institute for Chemical Research, Kyoto University
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抄録
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.
収録刊行物
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- Biomedical Research on Trace Elements
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Biomedical Research on Trace Elements 17 (4), 355-359, 2006
日本微量元素学会
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詳細情報 詳細情報について
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- CRID
- 1390001204366337664
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- NII論文ID
- 10018664330
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- NII書誌ID
- AN10423256
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- ISSN
- 18801404
- 0916717X
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- NDL書誌ID
- 8664426
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可