Structural highlights
Function
[PQQB_PSEPK] May be involved in the transport of PQQ or its precursor to the periplasm (By similarity).
Publication Abstract from PubMed
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 beta-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.
Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway.,Koehn EM, Latham JA, Armand T, Evans RL 3rd, Tu X, Wilmot CM, Iavarone AT, Klinman JP J Am Chem Soc. 2019 Mar 13;141(10):4398-4405. doi: 10.1021/jacs.8b13453. Epub, 2019 Feb 27. PMID:30811189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koehn EM, Latham JA, Armand T, Evans RL 3rd, Tu X, Wilmot CM, Iavarone AT, Klinman JP. Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway. J Am Chem Soc. 2019 Mar 13;141(10):4398-4405. doi: 10.1021/jacs.8b13453. Epub, 2019 Feb 27. PMID:30811189 doi:http://dx.doi.org/10.1021/jacs.8b13453
