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Fluoride Inhibition of Enolase: Crystal Structure and Thermodynamics ,
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The depletion of PEP highlights inhibition of the enolase enzyme, a previously identified target of NaF toxicity.
“highlighting the inhibition of the enolase enzyme (which catalyses the penultimate step of the EMP pathway, converting 3‐phosphoglycerate to PEP), one of the targets of NaF toxicity previously identified in in vitro studies (Qin et al., 2006).”
From Role of the CrcB transporter of Pseudomonas putida in the multi‐level stress response elicited by mineral fluoride (2022) · cites this paper as Qin et al., 2006
When in complex with a divalent metal ion and ADP, fluoride forms a non-functional mimic of ATP that can inhibit enolase.
“when in complex with a divalent metal ion and ADP, fluoride forms a non-functional mimic of ATP that can inhibit enolase (Curran et al., 1994; Qin et al., 2006)”
From Small Molecule Fluoride Toxicity Agonists (2015) · cites this paper as Qin et al., 2006
In enolase, fluoride complexes an active site Mg2+, displacing the substrate's carboxylate group.
“In enolase, the enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis, fluoride complexes an active site Mg2+, displacing the substrate’s carboxylate group(19–22) (Figure 2b).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [19]
Essential enzymes inhibited by fluoride include pyrophosphatase, proton translocating ATPases, and enolase.
“Essential enzymes shown to be inhibited by fluoride include pyrophosphatase (Baykov et al., 2000), proton translocating ATPases (Sutton et al., 1987; Sturr and Marquis, 1990) and enolase (Qin et al., 2006) (Fig. 5).”
From Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances (2022) · cites this paper as Qin et al., 2006
Enolase is inhibited by fluoride with a Ki value of ~80 μM.
“Enolase (which converts 2-phosphoglycerate to phosphoenolpyruvate, or PEP) is inhibited by fluoride with a Ki value of ~80 μM100.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [100]
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Cited by
Sorted by citations
Wackett, L. P. (2022) · Microbial Biotechnology · doi:10.1111/1751-7915.13928 · Cited by 165
Stockbridge, R. B., & Wackett, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-49018-1 · Cited by 80
Membrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
Calero, P., Gurdo, N., & Nikel, P. I. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16110 · Cited by 56
It takes acid, rather than ice, to freeze glucose
van den Berg, S. A. A., Thelen, M. H. M., Salden, L. P. W., van Thiel, S. W., & Boonen, K. J. M. (2015) · Scientific Reports · doi:10.1038/srep08875 · Cited by 49
Small Molecule Fluoride Toxicity Agonists
Nelson, J. W., Plummer, M. S., Blount, K. F., Ames, T. D., & Breaker, R. R. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.03.016 · Cited by 30
Dodge, A. G., Thoma, C. J., O’Connor, M. R., & Wackett, L. P. (2024) · mBio · doi:10.1128/mbio.02785-23 · Cited by 23
Metadata
- Authors
- Qin, J., Chai, G., Brewer, J. M., Lovelace, L. L., & Lebioda, L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-12-22
- Volume
- 45
- Issue
- 3
- Pages
- 793-800
- ISSN
- 0006-2960
- 1520-4995
- Cited by
- 97
- References
- 0
- Language
- en
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