What is it about?
3-Hydroxybenzoate 6-hydroxylase (3HB6H, EC 1.13.14.26) 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.
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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.
Perspectives
More insight into the evolutionary relationship and catalytic properties of flavin-dependent aromatic hydroxylases is of eminent importance for understanding enzyme dynamics.
Professor Willem J.H. van Berkel
Wageningen University
Read the Original
This page is a summary of: 3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Contains a Phosphatidylinositol Cofactor, Frontiers in Microbiology, June 2017, Frontiers,
DOI: 10.3389/fmicb.2017.01110.
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