Biomaterial Database

Fluoride inhibition of proton-translocating ATPases of oral bacteria. 1987

S V Sutton, and G R Bender, and R E Marquis

Department of Microbiology and Immunology, University of Rochester, New York 14642.

The ATPases of isolated membranes of lactic acid bacteria were found to be inhibited by fluoride in a complex manner. Among the enzymes tested, that of Streptococcus mutans GS-5 was the most sensitive to fluoride, and the initial rate of hydrolysis of ATP was reduced 50% by approximately 3 mM fluoride. The enzyme of Lactobacillus casei ATCC 4646 was the most resistant, and about 25 mM fluoride was required for 50% inhibition. The response to fluoride appeared to involve reversible, noncompetitive inhibition during short exposure to low levels of fluoride and nonreversible inhibition at higher fluoride levels. In addition, kinetic studies of the effects of fluoride on the enzymes of membranes of S. mutans and L. casei indicated that reversible inhibition was at least partly overcome at high levels of either ATP or Mg. The effects of pH on fluoride inhibition of ATPases were markedly different from the effects of pH on inhibition of acid/base regulation of intact cells by fluoride. It appeared that formation of HF was not required for inhibition of the ATPases. F1 ATPases isolated from the membranes by washing with buffers of low ionic strength proved to be less sensitive to fluoride than the membrane-associated F1F0 holoenzymes, and it was concluded that the F0 or membrane sector of the holoenzyme is involved in fluoride inhibition.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D007780	Lacticaseibacillus casei	A rod-shaped bacterium isolated from milk and cheese, dairy products and dairy environments, sour dough, cow dung, silage, and human mouth, human intestinal contents and stools, and the human vagina. L. casei is CATALASE positive.	Lactobacillus casei
D009055	Mouth	The oval-shaped oral cavity located at the apex of the digestive tract and consisting of two parts: the vestibule and the oral cavity proper.	Oral Cavity,Cavitas Oris,Cavitas oris propria,Mouth Cavity Proper,Oral Cavity Proper,Vestibule Oris,Vestibule of the Mouth,Cavity, Oral
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D003773	Dental Plaque	A film that attaches to teeth, often causing DENTAL CARIES and GINGIVITIS. It is composed of MUCINS, secreted from salivary glands, and microorganisms.	Plaque, Dental
D005459	Fluorides	Inorganic salts of hydrofluoric acid, HF, in which the fluorine atom is in the -1 oxidation state. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Sodium and stannous salts are commonly used in dentifrices.	Fluoride
D006180	Proton-Translocating ATPases	Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.	ATP Dependent Proton Translocase,ATPase, F0,ATPase, F1,Adenosinetriphosphatase F1,F(1)F(0)-ATPase,F1 ATPase,H(+)-Transporting ATP Synthase,H(+)-Transporting ATPase,H(+)ATPase Complex,Proton-Translocating ATPase,Proton-Translocating ATPase Complex,Proton-Translocating ATPase Complexes,ATPase, F(1)F(0),ATPase, F0F1,ATPase, H(+),Adenosine Triphosphatase Complex,F(0)F(1)-ATP Synthase,F-0-ATPase,F-1-ATPase,F0F1 ATPase,F1-ATPase,F1F0 ATPase Complex,H(+)-ATPase,H(+)-Transporting ATP Synthase, Acyl-Phosphate-Linked,H+ ATPase,H+ Transporting ATP Synthase,H+-Translocating ATPase,Proton-Translocating ATPase, F0 Sector,Proton-Translocating ATPase, F1 Sector,ATPase Complex, Proton-Translocating,ATPase Complexes, Proton-Translocating,ATPase, H+,ATPase, H+-Translocating,ATPase, Proton-Translocating,Complex, Adenosine Triphosphatase,Complexes, Proton-Translocating ATPase,F 0 ATPase,F 1 ATPase,F0 ATPase,H+ Translocating ATPase,Proton Translocating ATPase,Proton Translocating ATPase Complex,Proton Translocating ATPase Complexes,Proton Translocating ATPase, F0 Sector,Proton Translocating ATPase, F1 Sector,Triphosphatase Complex, Adenosine
D006863	Hydrogen-Ion Concentration	The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH	pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D001410	Bacillus megaterium	A species of bacteria whose spores vary from round to elongate. It is a common soil saprophyte.	Bacillus megatherium