3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii Contains a Phosphatidylinositol Cofactor
What is it about?
3-Hydroxybenzoate 6-hydroxylase (3HB6H, EC 126.96.36.199) is a FAD-dependent monooxygenase involved in the catabolism of aromatic compounds in soil microorganisms. 3HB6H is unique among flavoprotein hydroxylases in that it harbors a phospholipid ligand. Here, we produced Rj3HB6H in the host R. jostii RHA#2 by employing a newly developed actinomycete expression system. Biochemical and biophysical analysis revealed that Rj3HB6H contains phosphatidylinositol, a specific constituent of actinomycete membranes. Native mass spectrometry suggests that the lipid cofactor stabilizes monomer-monomer contact.
Why is it important?
Understanding the function of the phospholipid ligand of 3HB6H is important for getting a better understanding of the structure-function relationship of flavoprotein mono-oxygenases and will facilitate their biocatalytic application for the production of high-value compounds.
The following have contributed to this page: Professor Lubbert Dijkhuizen and Professor Willem J.H. van Berkel