Biochemistry of Selenium Compounds and Pyridoxal 5'-phosphate enzymes
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- Mihara Hisaaki
- Institute for Chemical Research, Kyoto University
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- Esaki Nobuyoshi
- Institute for Chemical Research, Kyoto University
Bibliographic Information
- Other Title
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- セレン化合物とピリドキサール5'-リン酸酵素の生化学
- セレン カゴウブツ ト ピリドキサール 5 リンサン コウソ ノ セイカガク
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Description
Pyridoxal 5'-phosphate-dependent enzymes, selenocysteine lyase (SCL) and cysteine desulfurase, occur in a variety of organisms. SCL catalyzes the decomposition of L-selenocysteine to form L-alanine and an enzyme-bound cysteine perselenide (Cys-Se) intermediate. Cysteine desulfurase catalyzes the same type of reaction as SCL but acts on L-cysteine as a substrate to form an cysteine persulfide (Cys-SH) on the active site residue. We carried out comparative studies between SCL and cysteine desulfurase to investigate functional and mechanistic characteristics of the family of the enzymes. Spectrum analyses showed that L-cysteine enters into the active site pocket of SCL but can not form an external aldimine complex with PLP. The formation of an external aldimine complex between SCL and L-selenocysteine requires the active-site nucleophile Cys375. Thus, Cys375 of SCL plays a central role in the discrimination between selenium and sulfur in a substrate and its analog.
Journal
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- VITAMINS
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VITAMINS 80 (12), 587-595, 2006
THE VITAMIN SOCIETY OF JAPAN
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Details 詳細情報について
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- CRID
- 1390001205701067264
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- NII Article ID
- 110006152692
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- NII Book ID
- AN00207833
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- ISSN
- 2424080X
- 0006386X
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- NDL BIB ID
- 8630553
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- CiNii Articles
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- Abstract License Flag
- Disallowed