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Fluoride is a strong and specific inhibitor of (asymmetrical) Ap4A hydrolases
Abstract
Fluoride acts as a noncompetitive, strong inhibitor of (asymmetrical) Ap 4 A hydrolases (EC 3.6.1.17). The K i values estimated for the enzymes isolated from seeds of some higher plants (yellow lupin, sunflower and marrow) are in the range of 2–3 μM and I 50 for the hydrolase from a mammalian tissue (beef liver) is 20 μM. The anion, up to 25 mM, does not affect the following other enzymes which are able to degrade the bis(5'‐nucleosidyl)‐oligophosphates: Escherichia coli (symmetrical) Ap 4 A hydrolase (EC 3.6.1.41), yeast Ap 4 A phosphorylase (EC 2.7.7.53), yellow lupin Ap 3 A hydrolase (EC 3.6.1.29) and phosphodiesterase (EC 3.1.4.1). None of halogenic anions but fluoride affects the activity of (asymmetrical) Ap 4 A hydrolases. Usefulness of the fluoride effect for the in vivo studies on the Ap 4 A metabolism is shortly discussed.
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Fluoride is highly inhibitory to metallo-enzymes, particularly those using magnesium.
“Fluoride is highly inhibitory to metallo‐enzymes, particularly those using magnesium.”
From Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances (2022) · cites this paper as Guranowski, 1990
The inhibition of specific enzymes by fluoride can be exceedingly strong, with KI values for some enzymes measured to be as low as 2 μM.
“The inhibition of specific enzymes can be exceedingly strong, with KI values for some enzymes measured to be as low as 2 μM (Guranowski, 1990).”
From Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances (2022) · cites this paper as Guranowski, 1990
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Wackett, L. P. (2022) · Microbial Biotechnology · doi:10.1111/1751-7915.13928 · Cited by 165
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
- Guranowski, A.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1990-03-26
- Volume
- 262
- Issue
- 2
- Pages
- 205-208
- ISSN
- 0014-5793
- 1873-3468
- Cited by
- 33
- References
- 0
- Language
- en
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