Abstract
Fluoroamino acids are among the most widely used analogues of naturally occurring compounds for biochemical and physiological research. Their molecular dimensions are approximately the same as those of the natural analogues because the van der Waals radius of the fluorine atom is only slightly larger than that of hydrogen (1.35 Å versus 1.20 Å) for which it is normally substituted. However, the electronegativity of fluorine is greater than that of hydrogen (4.0 versus 2.1), and so the C-F bond has more of an ionic character than the C-H bond with a higher bond energy of 105.4 kcal per mole compared with 98.8 kcal per mole (Pauling, 1960). Moreover, substitution of fluorine for hydrogen in organic compounds tends to enhance their hydrophilic properties. Despite these differences, fluoroamino acids can compete successfully with naturally occurring amino acids in many biochemical reactions, especially those reactions which do not lead to cleavage of the C-F bond. For example, the fluoroamino acid p-fluorophenylalanine (PFPA) can even be incorporated into proteins in place of phenylalanine. Enzymes usually discriminate against fluorosubstituted amino acids, but there are a few examples of enhanced reactivity due to substitution.
1. While this review was being written, the author’s work was supported in part by research grants R01 AM-08990 from the United States Public Health Service and GB-6573 from the U.S. National Science Foundation.
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References
Adelberg, E. A.: Selection of bacterial mutants which excrete antagonists of antimetabolites. J. Bact. 76, 326 (1958)
Ames, G.F.: Uptake of amino acids by Salmonella typhimurium. Arch. Bioehem. Biophys. 104, 1–18 (1964)
Atkinson, D.E., Melvtn, S., Fox, S.W.: Effects of p-fluorophenylalanine on the growth of Lactobacillus arabinosus. Arch. Bioehem. Biophys. 31, 205–211 (1951)
Baker, U.S., Jobnson, J.E., Fox, S.W.: Incorporation of p-fluorophenylalanine into proteins of Lactobacillus arabinosus. Biochim. biophys. Acta (Amst.) 28, 318–327 (1958)
Baltimore, D., Franklin, R.M., Callender, J.: Mengovirus-induced inhibition of host ribonucleic acid and protein synthesis. Biochim. biophys. Acta (Amst.) 76,425–430 (1963)
Bowman, W.H., Mallette, M.F.: Catabolism of p-fluorophenylalanine by Escherichia coli. Arch. Bioehem. Biophys. 117, 563–572 (1966)
Bowman, W.H., Palmer, I. S., Clagett, C. O., Mallette, M.F.: Effects of p-fluorophenylalanine on lactose-indueed-β-galactosidase synthesis in resting-cell suspensions of Escherichia coli. Arch. Bioehem. Biophys. 108, 314–322 (1964)
Brostrom, M.A., Binkley, S.B.: Membrane alteration and the formation of metachromatic granules in Escherichia coli treated with p-fluorophenylalanine. J. Bact. 98, 1263–1270 (1969a)
Brostrom, M.A., Binkley, S.B. Synchronous growth of Escherichia coli after treatment with fluorophenylalanine. J. Bact. 98, 1271–1273 (1969b)
Buchan, A., Burke, D.C.: Interferon production in chick-embryo cells. The effect of puro-mycin and p-fluorophenylalanine. Bioehem. J. 98, 530–536 (1966)
Carpenter, C, Binkley, S.B.: Effect of p-fluorophenylalanine on chromosome replication in Escherichia coli. J. Bact. 96, 939–949 (1968)
Chantrenne, H., Courtois, C.: Formation de catalase induite par l’oxygene chez la levure. Biochim. biophys. Acta (Amst.) 14, 397–400 (1954)
Cohen, G.N., Adelberg, E.A.: Kinetics of incorporation of p-fluorophenylalanine by a mutant of Escherichia coli resistant to this analogue. J. Bact. 76, 328–330 (1958)
Cohen, G.N., Halvorson, H.O., Spiegelman, S.: Effects of p-fluorophenylalanine on the growth and physiology of yeast. In R.B. Roberts (ed.), Microsomal Particles and Protein Synthesis, pp. 100–108. Oxford: Pergamon Press 1958
Cohen, G.N., Monod, J.: Bacterial permeases. Bact. Rev. 21, 169–194 (1957)
Cohen, G.N., Munier, R.: Effects des analogues structuraux d’amino acides sur la croissance, la synthèse de protéines et la synthèse d’enzymes chez Escherichia coli. Biochim. biophys. Acta (Amst.) 31, 347–356 (1959)
Cohen, G.N., Rickenberg, H.V.: Concentration spècifique réversible des amino acides chez Escherichia coli. Ann. Inst. Pasteur 91, 693–720 (1956)
Coleman, G., Elliott, W.H.: Studies on a-amylase formation by Bacillus subtilis. Bioehem. J. 83, 256–263 (1962)
Conway, T.W., Lansford, E.M., Jr., Shive, W.: Purification and substrate specificity of a phenylalanine activating enzyme from Escherichia coli 9723. J. biol. Chem. 237, 2850–2854 (1962)
Conway, T.W., Lansford, E.M., Jr., Shive, W. Influence of phenylalanine analogues upon bacterial accumulation and incorporation of phenylalanine. J. Bact. 85, 141–149 (1963)
Conway, T.W., Lansford, E.M., Jr., Shive, W. Inhibition of bacterial phenylalanine utilization and activation. Arch. Bioehem. Biophys. 107, 120–125 (1964)
Cowie, D.B., Cohen, G.N., Bolton, E.T., DeRobichon-Szulmajster, H.: Amino acid analog incorporation into bacterial proteins. Biochim. biophys. Acta (Amst.) 34, 39–46 (1959)
Dickie, N., Dennis, D.A., Thatcher, F.S.: Effect of p-fluorophenylalanine on radiation sensitivity in Escherichia coli. Canad. J. Microbiol. 14, 799–803 (1968)
Dunn, T.F., Leach, F.R.: Incorporation of p-fluorophenylalanine into proteins by a cell-free system. J. biol. Chem. 242, 2693–2699 (1967)
Emeis, C. C.: Haploidisierung von diploiden Hefen durch p-Fluorophenylalanin. Z. Naturforsch. 21b, 816–817 (1966)
Ezekiel, D.H.: Accumulation of ribonucleic acid in bacterial nuclear preparations during treatment of whole cells with 8-azaguanine, tetracyclines, and other inhibitors. J. Bact. 87, 755–760 (1964)
Ezekiel, D.H. Requirement for p-fluorophenylalanine activation in control of ribonucleic acid synthesis. Biochim. biophys. Acta (Amst.) 95, 48–53 (1965)
Fangman, W.L., Nass, G., Neidhardt, F.C.: Immunological and chemical studies of phenyl-alanyl sRNA synthetase from Escherichia coli. J. molec. Biol. 13, 202–219 (1965)
Ezekiel, D.H., Neidhardt, F. C.: Protein and ribonucleic acid synthesis in a mutant of Escherichia coli with an altered aminoacyl ribonucleic acid synthetase. J. biol. Chem. 239, 1844–1847 (1964a)
Fangman, W.L., Nass, G., Demonstration of an altered aminoacyl ribonucleic acid synthetase in a mutant of Escherichia coli. J. biol. Chem. 239, 1839–1843 (1964b)
Fenster, E.D., Anker, H.S.: Incorporation into polypeptide and charging on transfer ribonucleic acid of the amino acid analog 5’, 5’, 5’-trifluoroleucine by leucine auxotrophs of Escherichia coli. Biochemistry 8, 269–274 (1969)
Finch, L.R.: Adaption to amino acid-analogues. J. molec. Biol. 14, 591–592 (1965)
Fleming, R.W., Williams, F.D., Wailes, K.A.: Effects of p-fluorophenylalanine and chloramphenicol on chemotaxis in Escherichia coli. J. Bact. 94, 855–859 (1967)
Fowden, L., Lewis, D., Tristram, H.: Toxic amino acids: their action as antimetabolites. Advanc. Enzymol. 29, 89–163 (1967)
Freundlich, M., Trela, J.M.: Control of isoleucine, valine and leucine biosynthesis. VI. Effect of 5’, 5’, 5’-trifluoroleucine on repression in Salmonella typhimurium. J. Bact. 99, 101–106 (1969)
Friedman, R.M., Sonnabend, J. A.: Inhibition of interferon action by p-fluorophenylalanine. Nature (Lond.) 203, 366–367 (1964)
Gros, F., Gros, F.: Rôle des acides amines dans la synthèse des acides nucleique chez Escherichia coli. Exp. Cell Res. 14, 104–131 (1958)
Gutz, H.: Induction of mitotic segregation with p-fluorophenylalanine in Schizosaccharomyces pombe. J. Bact. 92, 1567–1568 (1966)
Halvorson, H.O., Cohen, G.N.: Incorporation des amino-acides endogenes et exogènes dans les protéines de la levure. Ann. Inst. Pasteur 95, 73–87 (1958)
Halvorson, H.O., Spiegelman, S.: The inhibition of enzyme formation by amino acid analogues. J. Bact. 64, 207–221 (1952)
Hardwick, W.A., Foster, J.W.: On the nature of sporogenesis in some aerobic bacteria. J. gen. Physiol. 35, 907–927 (1951–52)
Hardy, C, Binkley, S.B.: The effect of p-fluorophenylalanine on nucleic acid biosynthesis and cell division in Escherichia coli. Biochemistry 6, 1892–1898 (1967)
Horowitz, N.H., Fling, M., Macleod, H., Watanabe, Y.: Structural and regulative genes controlling tyrosinase synthesis in Neurospora. Cold Spr. Harb. Symp. quant. Biol. XXVI, 233–238 (1961)
Hummeler, K., Weoker, E.: Influence of p-fluorophenylalanine on poliovirus particles. Virology 24, 456–460 (1964)
Ikeda, K.: Inhibition of pyocin R formation by fluorophenylalanine. J. Biochem. (Tokyo) 61, 615–622(1967)
Ikeda, K., Egami, F.: Effects of antibiotics and antimetabolites on the induced formation of pyocin R. Z. aUg. Mikrobiol. 6, 219–225 (1966)
Jeantet, C, Gomes, R.A., Monier, R.: Effet de la p-fluorophenylalanine sur la formation des ribosomes chez Escherichia coli. Bull. Soc. Chim. biol. (Paris) 50, 473–489 (1968)
Joklik, W. K.: The multiplication of poxvirus DNA. Cold Spr. Harb. Symp. quant. Biol. XXVII, 199–208 (1962)
Kang, S., Markovitz, A.: Depression of alkaline phosphatase in Escherichia coli by p-fluoro phenylalanine. J. Bact. 94, 87–91 (1967a)
Kang, S., Markovitz, A. Induction of capsular polysaccharide synthesis by p-fluorophenylalanine in Escherichia coli wild type and strains with altered phenylalanyl soluble ribonucleic acid synthetase. J. Bact. 93, 584–591 (1967b)
Kang, S., Rockey, P., Markovitz, A.: Derepression of β-galaetosidase synthesis in Escherichia coli K-12 by p-fluorophenylalanine. J. Bact. 96, 139–145 (1968)
Kaplan, J. G.: The effect of inhibitors on the induction of cryptic and patent yeast catalase. Enzymologia 25, 359–366 (1962)
Katterman, R., Slonimski, P.P.: Differential effect of structural analogues of amino acids on the formation of respiratory enzymes induced by oxygen. C. R. Acad. Sci. (Paris) 250, 220–221 (1960)
Kempner, E.S., Cowie, D.B.: Metabolic pools and the utilization of amino acid analogs for protein synthesis. Biochim. biophys. Acta (Amst.) 42, 401–408 (1960)
Kepes, A.: Sequential transcription and translation in the lactose operon of Escherichia coli. Biochim. biophys. Acta (Amst.) 138, 107–123 (1967)
Kepes, A., Beguin, S.: Hydroxylamine, an inhibitor of peptide chain initiation. Biochem. biophys. Res. Commun. 18, 377–383 (1965)
Kerridge, D.: The effect of amino acid analogues on the synthesis of bacterial flagella. Biochim. biophys. Acta (Amst.) 31, 579–581 (1959)
Kerridge, D. The effect of inhibitors on the formation of flagella by Salmonella typhimurium. J. gen. Microbiol. 23, 519–538 (1960)
Kerridge, D. The effect of environment on the formation of bacterial flagella. Symp. Soc. gen. Microbiol. 11, 41–68 (1961)
Lark, K. G.: Regulation of chromosome replication and segregation in bacteria. Bact. Rev. 30, 3–32 (1966)
Lascelles, J.: Adaptation to form bacteriochlorophyll in Bhodopseudomonas spheroides: Changes in activity of enzymes concerned in pyrrole synthesis. Biochem. J. 72, 508–518 (1959)
Leick, V.: Effect of actinomycin D and DL-p-fluorophenylalanine on ribosome formation in Tetrahymena pyriformis. Europe. J. Biochem. 8, 215–220 (1969)
Lev, M.: Vitamin K deficiency in Fusiformis nigrescens. I. Influence on whole cells and cell envelope characteristics. J. Bact. 95, 2317–2324 (1968)
Lhoas, P.: Mitotic haploidization by treatment of Aspergillus niger diploids with para-fluorophenylalanine. Nature (Lond.) 190, 744 (1961)
Lettauer, U.Z., Revel, M., Stern, R.: Coding properties of methyl-deficient phenylalanine transfer RNA. Cold Spr. Harb. Symp. quant. Biol. XXXI, 501–514 (1966)
McCully, K.S., Forbes, E.: The use of p-fluorophenylalanine with ‘master strains’ of Aspergillus nidulans for assigning genes to linkage groups. Genet. Res. 6, 352–359 (1965)
Mitani, M., Iino, T.: Phenocopies of a heteromorphous flagellar mutant in Salmonella. J. Bact. 93, 766–767 (1967)
Moyed, H.S., Friedman, M.: Interference with feed back control: A mechanism of antimetabolite action. Science 129, 968–969 (1959)
Munier, R.: Substitution totale de la phénylalanine par To ou la m-fluorophénylalanine dans les protéines d’Escherichia coli. C.R. Acad. Sci. (Paris) 248, 1870–1873 (1959)
Munier, R., Cohen, G.N.: Incorporation d’analogues structuraux d’aminoacides dans les proteins bacteriennes. Biochim. biophys. Acta (Amst.) 21, 592–593 (1956)
Munier, R., Cohen, G.N. Incorporation d’analogues structuraux d’aminoacides dans les proteines bacteriennes au cours de leur synthese in vivo. Biochim. biophys. Acta (Amst.) 31, 378–391 (1959)
Munier, R., Drappier, A., Thommegay, C.: Substitution totale des analogues 5 et 6-fluorés du tryptophane à cet aminoacide dans les protéines d’Escherichia coli. Effect de cette incorporation, sur la biosynthèse d’ enzymes. C.R. Acad. Sci. (Paris) 265, 1429–1432 (1967)
Munier, R., Sarrazin, G.: Différence existant entre les propiétés de la β-galactosidase normale et celles de la β-galactosidase dont tous les groupes tyrosine sont remplaces par la 3-fluorotyrosine. C.R. Acad. Sci. (Paris) 259, 677–680 (1964)
Munier, R., Sarrazin, G. Substitution totale de la 3-fluorotyrosine à la tyrosine dans les protéines d’ Escherichia coli. C.R. Acad. Sci. (Paris) 256, 3376–3378 (1963)
Nisman, B., Hirsch, M.: Étude de I’activation et de Fincorporation des acides aminés par des fractions enzymatiques d’E. coli. Ann. Inst. Pasteur 95, 615–636 (1958)
Okuda, K., Edwards, G.C., Winnick, T.: Biosynthesis of gramicidin and tyrocidine in the Dubos strain of Bacillus brevis. I. Experiments with growing cultures. J. Bact. 85, 329–338 (1963)
Orgel, L.E.: Adaption to wide-spread disturbance of enzyme function. J. molec. Biol. 9, 208–212 (1964)
Pauling, L.: The Nature of the Chemical Bond. 3rd Ed. New York: Cornell Univ. Press 1960
Perkins, J. P., Louie, D.D., Aronson, J.N.: Effects of some amino acid analogues on Bacillus cereus sporulation using static and shaken cultures. Canad. J. Microbiol. 9, 791–797 (1963)
Pine, M.J.: Response of intracellular proteolysis to alteration of bacterial protein and the implications in metabolic regulation. J. Bact. 93, 1527–1533 (1967)
Polsinelli, M.: Linkage relations between genes for amino acid or nitrogenous base biosynthesis and genes controlling resistance to structurally correlated analogs. G. Microbiol. 13, 99–110(1965)
Previc, E., Binkley, S.: Repression and inhibition of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase by parafluorophenylalanine in Escherichia coli. Biochem. biophys. Res. Commun. 16, 162–166 (1964a)
Previc, E., Binkley, S. Slow exponential growth of Escherichia coli in presence of p-fluorophenylalanine. Effects of the analog on aromatic biosynthesis. Biochim. biophys. Acta (Amst.) 87, 277–290 (1964b)
Rapoport, G., Dedonder, R.: Synthèse de la lévane-sucrase chez Bacillus subtilis en presence d’analogues structuraux d’amino-acides. Biochim. biophys. Acta (Amst.) 89, 354–356 (1964)
Rasmussen, L.: Effects of DL-p-fluorophenylalanine on Paramecium aurelia during the cell generation cycle. Exp. Cell Res. 45, 501–504 (1967)
Rasmussen, L., Zeuthen”, E.: Cell division and protein synthesis in Tetrahymena, as studied with p-fluorophenylalanine. C.R. Lab. Carlsberg 32, 333–358 (1963)
Rennert, O.M., Anker, H.S.: On the incorporation of 5’, 5’, 5’ -trifluoroleucine into proteins of E. coli. Biochem. J. 2, 471–476 (1963)
Richmond, M.H.: Immunological properties of exopenicillinase synthesized by Bacillus cereus 569/H in the presence of amino acid analogues. Biochem. J. 77, 112–121 (1960a)
Richmond, M.H. Incorporation of DL-β-(p-fluorophenyl) [β-14C] alanine into exopenicillinase by Bacillus cereus 569/H. Biochem. J. 77, 121–135 (1960b)
Richmond, M.H. The effect of amino acid analogues on growth and protein synthesis in microorganisms. Bact. Rev. 26, 398–420 (1962)
Richmond, M.H. Random replacement of phenylalanine by p-fluorophenylalanine in alkaline phosphatase(s) formed during biosynthesis by E. coli. J. molec. Biol. 6, 284–294 (1963)
Richmond, M.H. The enzymic basis of specific antibacterial action by structural analogues. Biol. Rev. 40, 93–128 (1965)
St., Lawrence, P., Maling, B.D., Altwerger, L., Rachmeler, M.: Mutational alteration of permeability in Neurospora: Effects on growth and the uptake of certain amino acids and related compounds. Genetics 50, 1383–1402 (1964)
Samborski, D.J., Forsyth, F.R.: Inhibition of rust development on detached wheat leaves by metabolites, antimetabolites, and enzyme poisons. Canad. J. Bot. 38, 467–476 (1960)
Schaechter, M., Maaløe, O., Kjeldgaard, N.O.: Dependency on medium and temperature of cell size and chemical composition during balanced growth of Salmonella typhimurium. J. gen. Microbiol. 19, 592–606 (1958)
Scharff, M.D., Summers, D.F., Levintow, L.: Further studies on the effect of p-fluorophenylalanine and puromycin on polio virus replication. Ann. New York Acad. Sci. 130, 282–290 (1965)
Scharff, M.D., Thorén, M.M., McElvain, N.F., Levintow, L.: Interruption of poliovirus RNA synthesis by p-fluorophenylalanine and puromycin. Biochem. biophys. Res. Commun. 10, 127–132 (1963)
Shearn, A., Horowitz, N.H.: A study of transfer ribonucleic acid in Neurospora. I. The attachment of amino acids and amino acid analogs. Biochemistry 8, 295–303 (1969)
Shive, W., Skinner, C.G.: Amino acid analogues. In: R.W. Hochster and J.H. Quastel (Eds.), Metabolic Inhibitors, pp. 1–73. New York: Academic Press Inc. 1963
Sinha, U.: Aromatic amino acid biosynthesis and p-fluorophenylalanine resistance in Aspergillus nidulans. Genet. Res. 10, 261–272 (1967)
Smith, L.C., Ravel, J.M., Lax, S.R., Shive, W.: The effects of phenylalanine and tyrosine analogs on the synthesis and activity of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetases. Arch. Biochem. Biophys. 105, 424—430 (1964)
Sorsoli, W.A., Spence, K.D., Parks, L.W.: Amino acid accumulation in ethionine-resistant Saccharomyces cerevisiae. J. Bact. 88, 20–24 (1964)
Surdin, Y., Sly, W., Sire, J., Bordes, A.M., DeRobichon-Szulmajster, H.: Proprietes et contrôle génétique du système d’accumulation des acides aminés chez Saccharomyces cerevisiae. Biochim. biophys. Acta (Amst.) 107, 546–566 (1965)
Tanami, Y., Pollard, M.: Effect of p-fluorophenylalanine on psittacosis virus in tissue cultures. J. Bact. 83, 437–442 (1962)
Thang, M.N.: Rôle du chloramphenicol dans la synthese de l’ARN en presence des analogues d’acides aminés. Bull. Soc. Chim. biol. (Paris) 47, 573–583 (1965)
Thiebe, R., Zachau, H.G.: A specific modification next to the anticodon of phenylalanine transfer ribonucleic acid. Europe. J. Biochem. 5, 546–555 (1968)
Trela, J.M., Freundlich, M.: Uncoupling of protein and ribonucleic acid synthesis by 5’, 5’, 5’-trifiuoroleueine in Salmonella typhimurium. J. Bact. 99, 107–112 (1969)
van Andel, O.M.: Fluorophenylalanine as a systemic fungicide. Nature (Lond.) 194, 790 (1962)
Verwoerd, D.W., Hausen, P.: Studies on the multiplication of a member of the Columbia SK group (ME virus) in L cells. IV. Role of “early proteins” in virus induced metabolic changes. Virology 21, 628–635 (1963)
Waltho, J. A., Holloway, B.W.: Suppression of fluorophenylalanine resistance by mutation to streptomycin resistance in Pseudomonas aeruginosa. J. Bact. 92, 35–42 (1966)
Webster, R.E., Gross, S.R.: The a-isopropylmalate synthetase of Neurospora. I. The kinetics and end product control of a-isopropylmalate synthetase function. Biochem. J. 4, 2309–2318 (1965)
Welker, N.E., Campbell, L.L.: De novo synthesis of a-amylase by Bacillus stearothermo-philus. J. Bact. 86, 1202–1210 (1963)
Welker, N.E., Campbell, L.L. Preferential synthesis of a-amylase by Bacillus stearothermophilus in the presence of 5-methyl-tryptophan. J. Bact. 87, 828–831 (1964)
Winnick, R.E., Lis, BL, Winnick, T.: Biosynthesis of gramicidin S. I. General characteristics of the process in growing cultures of Bacillus brevis. Biochim. biophys. Acta (Amst.) 49, 451–462 (1961a)
Winnick, R.E., Winnick, T.: Biosynthesis of gramicidin S. II. Incorporation experiments with labeled amino acid analogs, and the amino acid activation process. Biochim. biophys. Acta (Amst.) 53, 461–468 (1961b)
Yoshida, A.: Studies on the mechanism of protein synthesis; Incorporation of p-fluoro-phenylalanine into a-amylase of Bacillus subtilis. Biochim. biophys. Acta (Amst.) 41, 98–103 (1960)
Zeuthen, E.: The temperature-induced division synchrony in Tetrahymena. In: E. Zeuthen (ed.), Synchrony in Cell Division and Growth, pp. 99–158. New York: Interscience Publishers 1964
Zeuthen, E., Rasmussen, L.: Incorporation of DL-p-fluorophenylalanine into proteins of Tetrahymena. J. Protozool., Suppl. 13, 29–30 (1966)
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Marquis, R.E. (1970). Fluoroamino Acids and Microorganisms. In: Smith, F.A. (eds) Pharmacology of Fluorides. Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology, vol 20 / 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-99973-4_5
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