Chaperone Function of Diol Dehydratase-Reactivase Revealed

January 27, 2014

Vitamin B12 is a coenzyme that binds to an activation site of enzyme and supports catalysis of the enzyme. Enzymes dependent on vitamin B 12 such as holodiol dehydratase often become inactivated when the bound vitamin B12 becomes damaged. Diol dehydratase-reactivase is a molecular chaperone that reactivates inactivated holodiol dehydratase by removing damaged vitamin B12 from holodiol dehydratase.
However, the reactivation mechanism was not fully understood.

The research group in Okayama University Graduate School of Natural Science and Technology has revealed the molecular mechanism of the chaperone for the reactivation of inactivive enzymes that are dependent on vitamin B12. They identified amino acids in the chaperone that have a major role in the interaction between the chaperone and the enzyme during the reactivation process.

The findings were published on December 3, 2013 in the journal of Biochemistry.

The chaperone function of diol dehydratase-reactivase could be applied to solve inactivation problems of enzymes that are dependent on vitamin B12.


Contact Information:
Mototaka Senda, Ph.D.
US Representative
Intellectual Property Office, Organization for Research Promotion and Collaboration, Okayama University
Fremont, California USA
TEL: 1-510-797-0907
Email: takasenda@okayama-u.ac.jp

Tetsuo Toraya, Ph.D.
Graduate School of Natural Science and Technology, Okayama University, Okayama Japan