Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway
| Autor: | Carrie M. Wilmot, Eric M. Koehn, Judith P. Klinman, Robert L. Evans, Tara Armand, Xiongying Tu, John A. Latham, Anthony T. Iavarone |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Protein family
Iron 010402 general chemistry Hydroxylation 01 natural sciences Biochemistry Cofactor Catalysis Article Mixed Function Oxygenases chemistry.chemical_compound Colloid and Surface Chemistry Biosynthesis Pyrroloquinoline quinone Bacterial Proteins Oxidoreductase Methylobacterium extorquens PQQ Cofactor chemistry.chemical_classification biology General Chemistry 0104 chemical sciences Quinone Dihydroxyphenylalanine Zinc chemistry Models Chemical biology.protein |
| Zdroj: | Journal of the American Chemical Society. 141(10) |
| ISSN: | 1520-5126 |
| Popis: | Understanding the biosynthesis of cofactors is fundamental to the life sciences, yet to date a few important pathways remain unresolved. One example is the redox cofactor pyrroloquinoline quinone (PQQ), which is critical for C1 metabolism in many microorganisms, a disproportionate number of which are opportunistic human pathogens. While the initial and final steps of PQQ biosynthesis, involving PqqD/E and PqqC, have been elucidated, the precise nature and order of the remaining transformations in the pathway are unknown. Here we show evidence that the remaining essential biosynthetic enzyme PqqB is an iron-dependent hydroxylase catalyzing oxygen-insertion reactions that are proposed to produce the quinone moiety of the mature PQQ cofactor. The demonstrated reactions of PqqB are unprecedented within the metallo β-lactamase protein family and expand the catalytic repertoire of nonheme iron hydroxylases. These new findings also generate a nearly complete description of the PQQ biosynthetic pathway. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|