Andrew Ulijasz
University of Alabama at Birmingham, AL·Microbiology & Immunology
Everyday metabolism makes toxic waste. Among the most abundant of these byproducts is glyoxal, a highly reactive molecule produced mainly during glycolysis, the pathway that breaks down sugar.
- Fields
Microbiology & Immunology
Biochemistry
Biophysics
- Topics
glyoxal
dicarbonyl stress
advanced glycation end products
- Grants
- 1 known grant, through Jan 2027
What they work on
- Map how GAD1, a heme-binding Antibiotic Monooxygenase domain protein, is regulated in Pseudomonas aeruginosa, including its co-transcription with GloA2, an enzyme that detoxifies glyoxal.
- Determine where GAD1 is distributed inside P. aeruginosa cells and identify its interactome, the set of partner proteins it binds, to test whether it redirects metabolism away from glycolysis.
- Solve the structures of GAD1 in its heme-free and heme-bound forms and in complex with interacting partners, to show how covalent glyoxal modification of the conserved residue Arg49 changes its behavior.
More about the research
Glyoxal chemically attacks specific amino acids in proteins, especially arginine, cysteine, histidine and lysine, degrading how those proteins work. In humans this dicarbonyl stress has been tied to cancer, diabetes, nervous system disorders, heart disease, hypertension, atherosclerosis and aging, and dedicated detoxifying systems exist across life because removing these molecules supports longevity. Even so, how a cell detects rising glyoxal and mounts a response is far less understood than oxidative stress.
Why it matters
Because this sensing pathway operates in the pathogen Pseudomonas aeruginosa, the genes and proteins uncovered could become new antimicrobial targets. GAD1-like proteins appear conserved up to humans, so the work may also clarify how human cells sense glyoxal buildup, an understudied stress linked to diabetes, cancer, heart disease and aging.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Rupal Gupta
College of Staten Island CUNY, NY·Biochemistry
Determine how 3-His iron-binding sites, an unusual alternative to the common 2-His-1-carboxylate motif, change the reaction mechanisms of non-heme iron enzymes that cut aromatic rings, using biochemical and spectroscopic methods.
Mohammad R Seyedsayamdost
Princeton University, NJ·Chemistry
Use high-throughput elicitor screening (HiTES) and genome-guided searches to uncover cryptic natural products in human microbiome bacteria, including radical SAM-modified peptides and selenium-containing metabolites.
Robert Clubb
University of California-Los Angeles, CA·Biochemistry
Determine how the C. diphtheriae surface receptor HbpA captures human hemoglobin, and test whether it works with other heme-binding receptors to distort hemoglobin and trigger heme release.
The school
University of Alabama at Birmingham: 45 labs on PI Pages, $866M a year on research, 166 research doctorates a year.
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