Jake Enzman | 2026 I.S. Symposium
狈补尘别:听Jake Enzman
罢颈迟濒别:听Structural and Kinetic Evidence of Maleamate Amidohydrolase (NicF) in the Bacillus niacini Nicotinic Acid Catabolic Pathway
惭补箩辞谤:听Biochemistry and Molecular Biology
础诲惫颈蝉辞谤:听Mark Snider
N-Heterocyclic aromatic compounds (NHACs) are pervasive environmental pollutants found in herbicides, pesticides, and dyes. As NHACs can possess carcinogenic and toxic properties, it is critical to develop strategies to remove them from the environment. Bioremediation, the use of microorganisms to degrade harmful compounds, has emerged as a promising approach. Bacterial species such as Bacillus niacini and Bordetella bronchiseptica can degrade the NHAC nicotinic acid (NA), so the breakdown of NA functions as a model system for NHAC bioremediation. While the proteins responsible for NA degradation have been identified in B. niacini, the compounds that NA is broken down into remain unclear. Previous research suggests that these molecules may be similar to others found in analogous bacterial or fungal pathways of NA degradation. The goal of this project is to better understand a B. niacini enzyme (NicF) involved in the breakdown of NA, which will provide insight into the overall pathway of NA degradation in this bacterium. Computational approaches were used to predict the structure and to identify important amino acids within the enzyme. Experimental methods were then used to identify maleamic acid (MAA) as the compound broken down by NicF and to determine that this reaction occurs at biologically relevant rates. This project provides a better understanding of the scope of NHACs broken down by bacteria and identifies amino acids in the enzyme that are critical in its degradation of maleamic acid in B. niacini.
Posted in Symposium 2026 on May 1, 2026.
