Biotin synthase mechanism: on the origin of sulphur

FEBS Letters

Méjean, Annick²  Fournier, Françoise¹  Tse Sum Bui, Bernadette²  Florentin, Dominique²  Marquet, Andrée²  Ploux, Olivier² 

[1] Laboratoire de Chimie Structurale Organique et Biologique, Université Paris VI – CNRS UMR 7613, 4 place Jussieu, 75252 Paris Cedex 05, France;Laboratoire de Chimie Organique Biologique, Université Paris VI – CNRS UMR 7613, 4 place Jussieu, 75252 Paris Cedex 05, France

关键词: Biotin synthase;    Iron-sulfur cluster;    34S reconstituted enzyme;    Sulfur donor;    (FeS);    iron-sulphur cluster;    AdoMet;    S-adenosylmethionine;    DTT;    dithiothreitol;    DTB;    dethiobiotin;    Ado-CH2 ⋅;    deoxyadenosyl radical;    PFL;    pyruvate formate lyase;    ARNR;    anaerobic ribonucleotide reductase;    LAM;    lysine 2;    3-aminomutase;   

DOI  :  10.1016/S0014-5793(98)01464-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Biotin synthase catalyses the last step of the biosynthesis of biotin in microorganisms and plants. The active protein isolated from Bacillus sphaericus and Escherichia coli contains an iron-sulphur (FeS) cluster. The native enzymes were depleted of their iron and inorganic sulphide and the resulting apoenzymes were chemically reconstituted with FeCl₃ and Na₂[³⁴S] to give labelled (Fe³⁴S) enzymes. These enzymes were functional and when assayed in vitro produced labelled biotin containing about 65% of ³⁴S. These data strongly support the hypothesis that the sulphur of biotin is derived from the (FeS) centre of the enzyme.

【 授权许可】

Unknown