The effect of sodium monofluorophosphate on the enzymes phosphorylase and phosphatase

Rapp, G.W.; Sliwinski, R.

doi:10.1016/0003-9861(56)90440-4

Cited by 9 publications

(4 citation statements)

References 12 publications

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“…Alkaline phosphatases from various sources are strongly inhibited by MFP [Rapp and Sliwinski, 1956;Fernley and Walker. 1967], When MUP is a substrate for the calf intestinal enzyme, MFP and a range of other phosphate compounds all result in a raised K", and a lowered maximum rate of substrate hydrolysis.…”

Section: Inhibition Where Mfp May Be a Reaction Substrate Or Productmentioning

confidence: 99%

“…The latter shows satu ration kinetics, and has a similar K, of 5.5 mM, suggesting that MFP interacts at the active site of the phosphatase. MFP has no irreversible inhibitory effect on this en zyme in hepatocytes when added to an incu bation medium containing intact cells, but is inhibitory in broken cells [Shahed et al, 1981], Phosphorylase from potatoes shows com petitive inhibition with respect to ortho phosphate [Rapp and Sliwinski, 1956]. In teraction with a phosphorylase has been confirmed by Parrish et al [1977], who found that skeletal muscle apophosphorylase b, reconstituted with pyridoxal instead of its normal cofactor pyridoxal 5'-phosphate, is activated by either MFP or phos phite.…”

Section: Inhibition Where No Donor or Acceptor (F) Role Is Establishedmentioning

confidence: 99%

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Biochemistry of Monofluorophosphate

Pearce¹

1983

Caries Res

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Monofluorophosphate (MFP) can be synthesized in vitro by the transfer of a phosphoryl group from ATP to F^-, catalyzed by pyruvate kinase, or by the autocatalytic transfer of a phosphoryl group from the enzyme phosphoglucomutase. There is, however, no evidence that MFP is a normal intermediate in cell metabolism. MFP can be degraded by both alkaline and acid phosphatases, and the mechanism is probably similar to the hydrolysis or transfer of phosphoryl groups from other phosphatase substrates. MFP competitively inhibits pyruvate kinase and alkaline phosphatase, and irreversibly inhibits phosphorylase phosphatase. The possibility that impurities or hydrolysis products are responsible for reported effects makes the interpretation of many inhibition studies difficult. The widespread therapeutic use of MFP presents a strong case for a more detailed study of its metabolism.

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Section: Inhibition Where Mfp May Be a Reaction Substrate Or Productmentioning

confidence: 99%

Section: Inhibition Where No Donor or Acceptor (F) Role Is Establishedmentioning

confidence: 99%

Biochemistry of Monofluorophosphate

Pearce¹

1983

Caries Res

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“…Yang & Miller (91) attributed this increased oxygen uptake to an in creased utilization of ATP. The enzyme adenosine triphosphatase, which breaks down ATP, has been reported to be inhibited by fluorine (65). Fail ure of ATP to be broken down could account for the .…”

Section: Metabolic Effectsmentioning

confidence: 99%

Fluorides as Air Pollutants Affecting Plants

Treshow¹

1971

Annu. Rev. Phytopathol.

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“…enzymes that catalyze reactions of phosphorus compounds in plants are inhibited in vitro by fluoride or fluorophosphate. Included are enolase (Miller, 1958; Warburg and Christian, 1942), phosphoglucomutase (Chung and Nickerson, 1954;Yang and Miller, 1963), phosphatases (Bailey and Webb, 1944;Wildman and Bonner, 1947), and phosphorylases (Rapp and Sliwinski, 1956). However, attempts to detect these inhibitions in intact plants or to show that effects of fluoride on plants are related to inhibition of specific enzymes have been inconclusive.…”

Section: Severalmentioning

confidence: 99%