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Demonstration of a "channeling"mechanism in the biosynthetic pathway of vitamin B8 in plants


In collaboration with IBS, we have biochemically characterized the bifunctional enzyme BIO3-BIO1 from Arabidopsis and solved its three-dimensional structure. Data concerning bifunctional enzyme catalyzing (or not) two successive stages of the same biosynthetic pathway are rare. This study is therefore essential from a fundamental point of view, but will also improve the production processes of molecules with high added value. This will also, in a more targeted way, enable the design of specific inhibitors aimed at therapeutic or pesticide purposes.

Published on 26 April 2012
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Three-dimensional structure of the bifunctional enzyme BIO3-BIO1 of Arabidopsis thaliana. The two domains BIO1 and BIO3 are visible, as well as molecules of DAPA, the reaction intermediate, migrating from the BIO1 site where it is synthesized to the BIO3 site or it will be transformed into DTB, the direct precursor of biotin.

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