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Bacterial Degradation of Nτ-Methylhistidine
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    Bacterial Degradation of Nτ-Methylhistidine
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    ACS Chemical Biology

    Cite this: ACS Chem. Biol. 2022, 17, 7, 1989–1995
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    https://doi.org/10.1021/acschembio.2c00437
    Published June 27, 2022
    Copyright © 2022 American Chemical Society

    Abstract

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    The first three enzymatic steps by which organisms degrade histidine are universally conserved. A histidine ammonia-lyase (EC 4.3.1.3) catalyzes 1,2-elimination of the α-amino group from l-histidine; a urocanate hydratase (EC 4.2.1.49) converts urocanate to 4-imidazolone-5-propionate, and this intermediate is hydrolyzed to N-formimino-l-glutamate by an imidazolonepropionase (EC 3.5.2.7). Surprisingly, despite broad distribution in many species from all kingdoms of life, this pathway has rarely served as a template for the evolution of other metabolic processes. The only other known pathway with a similar logic is that of ergothioneine degradation. In this report, we describe a new addition to this exclusive collection. We show that the firmicute Bacillus terra and other soil-dwelling bacteria contain enzymes for the degradation of Nτ-methylhistidine to l-glutamate and N-methylformamide. Our results indicate that in some environments, Nτ-methylhistidine can accumulate to concentrations that make its efficient degradation a competitive skill. In addition, this process describes the first biogenic source of N-methylformamide.

    Copyright © 2022 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acschembio.2c00437.

    • Detailed descriptions of all experiments, SDS PAGE of purified proteins, Michaelis–Menten kinetics of BtHAL, activity screen of Nτ-methylhistidase, IE-HPLC traces, RP-HPLC ESI-HR-MS analysis, sequence alignment of histidases, and list of bacterial species (PDF)

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    Cited By

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    This article is cited by 5 publications.

    1. Camille M. Vasseur, Dishani Karunasegaram, Florian P. Seebeck. Structure and Substrate Specificity of S-Methyl Thiourocanate Hydratase. ACS Chemical Biology 2024, 19 (3) , 718-724. https://doi.org/10.1021/acschembio.3c00745
    2. Zhe Zhou, Stavroula K. Hatzios. Microbial metabolism of host-derived antioxidants. Current Opinion in Chemical Biology 2025, 84 , 102565. https://doi.org/10.1016/j.cbpa.2024.102565
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    4. Francisco Manuel Salas-Garrucho, Alba Carrillo-Moreno, Lellys M. Contreras, Felipe Rodríguez-Vico, Josefa María Clemente-Jiménez, Francisco Javier Las Heras-Vázquez. Exploring the Kinetics and Thermodynamics of a Novel Histidine Ammonia-Lyase from Geobacillus kaustophilus. International Journal of Molecular Sciences 2024, 25 (18) , 10163. https://doi.org/10.3390/ijms251810163
    5. Giovanni Di Bonaventura, Carla Picciani, Veronica Lupetti, Arianna Pompilio. Comparative Proteomic Analysis of Protein Patterns of Stenotrophomonas maltophilia in Biofilm and Planktonic Lifestyles. Microorganisms 2023, 11 (2) , 442. https://doi.org/10.3390/microorganisms11020442

    ACS Chemical Biology

    Cite this: ACS Chem. Biol. 2022, 17, 7, 1989–1995
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acschembio.2c00437
    Published June 27, 2022
    Copyright © 2022 American Chemical Society

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