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Mechanism, Structure, and Inhibition of N-Monooxygenases

Award Number: R15GM164647
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 06/01/2026
PERIOD OF PERFORMANCE END DATE: 05/31/2029

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Mechanism, Structure, and Inhibition of N-Monooxygenases - Project Summary Many pathogenic bacteria and fungi require iron from the host to establish infection. A deep understanding of iron acquisition mechanisms is crucial for unraveling the principles of pathogenicity and could lead to innovative drug design strategies to tackle antibiotic resistance. One key aspect of iron acquisition is the secretion of low- molecular-weight, iron-scavenging molecules known as siderophores. This project focuses on investigating enzymes that catalyze a critical step in the biosynthesis of hydroxamate-containing siderophores. Flavin-dependent N-monooxygenases play a central role in this process by introducing hydroxyl groups onto the amino acid building blocks of siderophores, which ultimately contribute to the iron-chelating hydroxamate functional groups in the mature siderophore. These enzymes are essential for virulence in pathogenic organisms such as the fungus Aspergillus fumigatus and bacteria like Acinetobacter baumannii. This foundational study establishes a framework for investigating the structure, catalytic mechanism, and inhibition of flavin-dependent N-monooxygenases. In this proposal, we aim to: (1) perform detailed biochemical and structural studies of histamine N-monooxygenases from pathogenic bacteria, (2) identify and characterize inhibitors of the ornithine N-monooxygenase from A. fumigatus (SidA), and (3) structurally characterize elusive intermediates in the reaction catalyzed by SidA. The project will serve as an excellent platform for training undergraduate students in protein chemistry, enzyme characterization, inhibitor design and validation, and structural biochemistry. The successful completion of these aims will enhance our understanding of the molecular basis of siderophore- mediated iron assimilation and generate lead compounds for future drug development.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2026 ( Subtotal = $528,560 )
2026	2026	UNIVERSITY OF MISSOURI SYSTEM	300 W. 12TH STREET	ROLLA	MO	65409	PHELPS	USA	Biomedical Research and Research Training	000	1	5/11/2026	NEW	$528,560
														Subtotal = $528,560

Grand Total All Awards = $528,560

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Mechanism, Structure, and Inhibition of N-Monooxygenases

Award Number: R15GM164647

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 06/01/2026

PERIOD OF PERFORMANCE END DATE: 05/31/2029

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