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Project Area: Understanding P450 mediated Vitamin-D metabolism
Project Area: Understanding P450 mediated Vitamin-D metabolism
We seek to use a combination of biochemistry and biophysical techniques to understand the structural biology of vitamin-D metabolism. Vitamin-D is activated and inactivated by a series of cytochrome P450 enzymes. Furthering our understanding of how site-specific hydroxylation occurs in these pathways has the potential to advance therapeutics that address human vitamin D insufficiencies. Specific topics include i) understanding how vitamin D metabolizing enzymes in mitochondria (like CYP24A1 and CYP11A1) undergo protein-protein interactions in support of their function, and ii) how do these enzyme specifically recognize the form of vitamin D and the site of activity?
We seek to use a combination of biochemistry and biophysical techniques to understand the structural biology of vitamin-D metabolism. Vitamin-D is activated and inactivated by a series of cytochrome P450 enzymes. Furthering our understanding of how site-specific hydroxylation occurs in these pathways has the potential to advance therapeutics that address human vitamin D insufficiencies. Specific topics include i) understanding how vitamin D metabolizing enzymes in mitochondria (like CYP24A1 and CYP11A1) undergo protein-protein interactions in support of their function, and ii) how do these enzyme specifically recognize the form of vitamin D and the site of activity?
Project Area: Undestanding P450 from pathogenic bacteria
Project Area: Undestanding P450 from pathogenic bacteria
The enzyme CYP121 is essential for the bacterium that causes Tuberculosis. CYP121 mediates an unusual phenol-coupling reaction on the dipeptide dicyclotyrosine. Here we aim to understand CYP121 function by studying changes in protein conformation. We recently demonstrated that the enzyme relies on formation of dimers to appropriately bind its substrate and perform catalysis. This project was also the first reported use of 19F-NMR to study cytochrome P450 structure.
The enzyme CYP121 is essential for the bacterium that causes Tuberculosis. CYP121 mediates an unusual phenol-coupling reaction on the dipeptide dicyclotyrosine. Here we aim to understand CYP121 function by studying changes in protein conformation. We recently demonstrated that the enzyme relies on formation of dimers to appropriately bind its substrate and perform catalysis. This project was also the first reported use of 19F-NMR to study cytochrome P450 structure.
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