Document Type
Poster
Publication Date
Summer 2025
Abstract
3-Hydroxyisobutyrate dehydrogenase (HIBDH) is an important enzyme in the valine degradation pathway across many organisms. HIBDH oxidizes 3-hydroxyisobutyrate to methylmalonate semialdehyde and 3-hydroxypropionate to malonate semialdehyde, all within the process of converting valine ultimately into acetyl-CoA which is responsible for energy production under extended periods of darkness. While its role in valine degradation is known the relationship between HIBDH’s structure and function is not necessarily as well understood in plants. As such, the Kerry Rouhier lab has taken on the task of performing single-point mutations to determine how different amino acids alter the structure and function of HIBDH in comparison to a non-mutated, “wild-type” (wt) version. This allows us to determine which amino acids play key roles in HIBDH’s structure and function. This summer, I was responsible for purifying 10 of the more than 20 mutated proteins and assessing their enzyme activity (function). Concurrent work in the lab is investigating potential structural changes. Altogether, this data on the structure and function of mutations of HIBDH will help the entire scientific community to better understand how HIBDH works and what it needs to function.
Recommended Citation
Hoffman, Kieran and Rouhier, Kerry A., "Purification of Arabidopsis thaliana 3-Hydroxyisobutyrate Dehydrogenase for Structure-Function Studies" (2025). Kenyon Summer Science Scholars Program. Paper 770.
https://digital.kenyon.edu/summerscienceprogram/770
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