3o3m

Structural highlights

Function

HADB_CLODI Involved in the reductive branch of L-leucine fermentation. Catalyzes the irreversible beta/alpha-elimination of water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. This beta/alpha-dehydration depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. The enzyme is specific for the R-isomer.^{[1] [2]}

References

1. ↑ Kim J, Darley D, Buckel W. 2-Hydroxyisocaproyl-CoA dehydratase and its activator from Clostridium difficile. FEBS J. 2005 Jan;272(2):550-61. doi: 10.1111/j.1742-4658.2004.04498.x. PMID:15654892 doi:http://dx.doi.org/10.1111/j.1742-4658.2004.04498.x
2. ↑ Knauer SH, Buckel W, Dobbek H. Structural Basis for Reductive Radical Formation and Electron Recycling in (R)-2-Hydroxyisocaproyl-CoA Dehydratase. J Am Chem Soc. 2011 Mar 2. PMID:21366233 doi:10.1021/ja1076537