The Inhibiting Effect of Sodium Fluoride on the Action of Lipase

Loevenhart, A. S.; Peirce, George J.

doi:10.1016/s0021-9258(17)46027-3

Cited by 27 publications

(4 citation statements)

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“…The procedure given here is similar to that of Loevenhart et al (1,6), except for the addition of ethyl alcohol as suggested by Schlamowitz (8) and the shortened incubation time. Ethyl alcohol is added before the titration to inhibit further enzymatic hydrolysis, as hydrolysis is still proceeding at the end of the incubation period.…”

Section: Discussionmentioning

confidence: 94%

Estimation of Small Amounts of Fluoride in Body Fluids

Linde¹

1959

Anal. Chem.

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Section: Discussionmentioning

confidence: 94%

Estimation of Small Amounts of Fluoride in Body Fluids

Linde¹

1959

Anal. Chem.

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“…Fluoride affects the enzymes involved in cellular metabolic pathways due to ubiquitous fluoride activity in biological systems. Starting in the late 1800s, sodium fluoride was identified as a lipase inhibitor before its discovery in preventing dental caries 1,2 . As of 2018, the protein databank has collected over 700 proteins crystallized in complex with fluoride 3 .…”

Section: Introductionmentioning

confidence: 99%

“…Starting in the late 1800s, sodium fluoride was identified as a lipase inhibitor before its discovery in preventing dental caries. 1,2 As of 2018, the protein databank has collected over 700 proteins crystallized in complex with fluoride. 3 Over 100 of these have had separate, independent enzymatic studies targeting phosphatases, kinases, hydrolases, and other metalloproteins for fluoride inhibition in vitro.…”

mentioning

confidence: 99%

An in‐silico investigation of fluoride ions impact on pancreatic lipase

Yadav

Basha²,

Pindi

2022

J of Cellular Biochemistry

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Fluorine is a halogen beneficial to teeth and bones at a lower concentration. But in excess, it is a toxin and causes adverse effects. Fluoride is toxic to enzymes generally when it inhibits the enzyme activity involved in metabolic pathways. Here we study invitro and invivo findings on the interaction of fluoride on the enzymes Aconitase, Adenylyl cyclase, Arginase, Cytochrome‐c‐oxidase, Glucose‐6‐phosphatase, Protein phosphatase, Succinate dehydrogenase from liver and lipase from pancreas by using molecular docking and simulations to gain insights into the mechanism by which fluoride modifies the activity of pancreatic lipase. our molecular modeling and docking studies identified that lipase is the most strongly inhibited enzyme compared to other enzymes mentioned above with −0.42 Kcal/mol binding energy and 495.78 milli molar of predicted IC50 value with interaction with Phe227 residue. To further validate this, we have taken the lipase enzyme in presence of fluoride ions for molecular dynamic simulations of 100 ns. To analyze the impact of fluoride ions on the lipase dynamics, two different simulations of 100 ns each were performed. In one simulation, we have simulated lipase in its apo form in the aqueous environment without any fluoride ions and in another simulation lipase in its apo form was kept in the presence of randomly placed fluoride ions countered with sodium ions to maintain the pH as neutral. The simulation analysis revealed that major fluctuations in lipase was observed between 230 and 300 residues in presence of fluoride ions. Interestingly, this is the exact location of the “lid” like acting loop of residues responsible for the inward/outward movement of the substrate to lipase catalytically active site containing catalytic triad of residues Leu153, His263, and Pro177. His263 residue random flip is believed to be the critical incident that causes the substrate's inward/outward movement at the catalytically active site coordinated by “lid” opening, providing enough space for the substrate.

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“…It was found that inhibition by fluoride did not increase and may have dropped somewhat. The enzyme activity itself also suffered a small decrease which probably resulted from inactivation of the enzyme by acid (7).…”

mentioning

confidence: 99%