Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K

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公開日
2006-07-24
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1016/j.febslet.2006.07.051
公開者
Wiley

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説明

<jats:p>Thiocyanate hydrolase (SCNase) is a cobalt‐containing enzyme with a post‐translationally modified cysteine ligand, γCys131‐SO<jats:sub>2</jats:sub>H. When the SCNase α, β and γ subunits were expressed in <jats:italic>Escherichia coli</jats:italic>, the subunits assembled to form a hetero‐dodecamer, (αβγ)<jats:sub>4</jats:sub>, like native SCNase but exhibited no catalytic activity. Metal analysis indicated that SCNase was expressed as an apo‐form irrespective of the presence of cobalt in the medium. On the contrary, SCNase co‐expressed with P15K, encoded just downstream of SCNase genes, in cobalt‐enriched medium under the optimized condition (SCNase<jats:sub>(+P15K)</jats:sub>) possessed 0.86 Co atom/αβγ trimer and exhibited 78% of the activity of native SCNase. SCNase<jats:sub>(+P15K)</jats:sub> showed a UV–Vis absorption peak characteristic of the SCNase cobalt center. About 70% of SCNase<jats:sub>(+P15K)</jats:sub> had the γCys131‐SO<jats:sub>2</jats:sub>H modification. These results indicate that SCNase<jats:sub>(+P15K)</jats:sub> is the active holo‐SCNase. P15K is likely to promote the functional expression of SCNase probably by assisting the incorporation of cobalt ion.</jats:p>

収録刊行物

  • FEBS Letters

    FEBS Letters 580 (19), 4667-4672, 2006-07-24

    Wiley

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