Liberal Arts and Sciences
Angerhofer Lab
Led by Alexander Angerhofer · Chemistry
What we study
The Angerhofer Lab studies how the manganese enzyme oxalate decarboxylase works by using electron paramagnetic resonance (a technique that detects magnetic properties of electrons) and structural analysis. They combine protein engineering, including unnatural amino acids, with chemistry, molecular biology, and bioinformatics tools to understand and improve the enzyme.
What working here is like
- Wet lab
- Computational
- Bacteria & microbes
- No organisms (data only)
- Coding required
- Projects
- 4
- Papers
- 3
Current projects
Investigation of Structure-Function Relation of Oxalate Decarboxylase
The lab studies an enzyme from Bacillus subtilis that breaks down oxalate. By making a shorter version that forms a trimer, they examine how shape affects activity, aiming to improve treatments for kidney stones and paper production.
From the Spring 2025 UF Undergraduate Research Symposium · abstract book, p. 471
Using Directed Evolution to Improve the Optimum pH of Oxalate Decarboxylase from Bacillus subtilis
Researchers created many mutated versions of an enzyme that breaks down oxalate and identified some that work better at higher pH; these promising variants are now being sequenced for further study.
From the Spring 2025 UF Undergraduate Research Symposium · abstract book, p. 357
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QM/MM Simulations for Determining and Visualizing OxDC
The project uses computer simulations to study how the enzyme oxalate decarboxylase (OxDC) binds its substrate, which is important for preventing kidney stones. Students will run quantum mechanics/molecular mechanics calculations to decide whether the enzyme binds the substrate in one or two places, and will analyze the binding energetics and reaction pathways.
From the Spring 2025 UF Undergraduate Research Symposium · abstract book, p. 351
Nanoencapsulation of Oxalate Decarboxylase for Improved Activity
The lab studied an enzyme that breaks down oxalate and tried to protect it with a tiny polymer shell. The student made the nanocapsules, measured their size, charge and mass, and tested activity, finding higher activity and better heat stability up to 55 °C compared to the plain enzyme.
From the Spring 2025 UF Undergraduate Research Symposium · abstract book, p. 242
Summaries are written by AI in plain language from public symposium abstracts and may be imperfect.
Recent papers, explained
- Bidentate Substrate Binding Mode in Oxalate Decarboxylase
2024 · Molecules
Investigating how oxalate decarboxylase binds its substrate with two points of attachment.
- Selective incorporation of 5‐hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase
2022 · Protein Science
Testing how adding 5‑hydroxytryptophan stops long‑range electron transfer in the enzyme.
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- Oxalate decarboxylase uses electron hole hopping for catalysis
2021 · Journal of Biological Chemistry
Studying electron hole hopping as the catalytic mechanism of oxalate decarboxylase.
Plain-language summaries are AI-written and reviewed by us; check the paper for details.
How to reach out
Alexander Angerhofer hasn't set up this page yet. Their UF Scholars profile lists their publications.