Structural and biochemical characterization of 3-hydroxybenzoate 6-hydroxylase
The thesis deals with the characterization of a new flavoprotein hydroxylase 3 hydroxybenzoate 6-hydroxylase (3HB6H) from Rhodococcus jostii RHA1. 3HB6H is able to insert exclusively oxygen in para-position and the enzyme has been chosen to study the structural basis of such regioselectivity. As main result, functional mirror image active sites direct regioselective 3-hydroxybenzoate hydroxylation. Moreover, the nature and role of unprecedented phospholipid binding has been analyzed demonstrating a role in enzyme oligomerization and a possible protective role during catalysis. To conclude, the knowledge acquired improves our insight into the strategies of flavin-dependent regioselective hydroxylation and the results emerged in this thesis provide a foundation for further structural and kinetic studies on 3HB6H and related enzymes.
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| Format: | Doctoral thesis biblioteca |
| Language: | English |
| Subjects: | biochemistry, molecular conformation, unspecific monooxygenase, aspecifiek mono-oxygenase, biochemie, moleculaire structuur, |
| Online Access: | https://research.wur.nl/en/publications/structural-and-biochemical-characterization-of-3-hydroxybenzoate- |
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