The Inhibition of Microbiological Growth by Allylglycine, Methallylglycine and Crotylglycine<sup>1,2</sup>

Dittmer, Karl; Goering, Harlan L.; Goodman, Irving; Cristol, Stanley J.

doi:10.1021/ja01187a057

Cited by 28 publications

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“…Similar results were obtained after administration of DL-C-allylglycine. This synthetic amino acid was shown to be a competitive analog of cysteine and inhibitor of bacterial growth, probably due to the similarity of its vinylene group to the divalent sulfur atom of cysteine [31].…”

Section: Substratementioning

confidence: 99%

Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Orłowski

Wilk

1975

Eur J Biochem

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y-Glutamyl transpeptidase, y-glutamyl cyclotransferase, L-pyrrolidone carboxylate hydrolase, y-glutamylcysteine synthetase and glutathione synthetase, the enzymes of the y-glutamyl cycle, were found in mouse brain, liver and kidney. The activity of L-pyrrolidone carboxylate hydrolase was many times lower than the activities of the other enzymes, and thus the conversion of L-pyrrolidone carboxylate to L-glutamate is likely to be the rate-limiting step of the cycle. The specificity of y-glutamyl cyclotransferase from mouse tissues was similar to that from rat tissues. The concentration of pyrrolidone carboxylate and y-glutamyl amino acids, intermediates of the y-glutamyl cycle, was determined by a gas chromatographic procedure coupled with electron capture detection. Administration of ~-2-aminobutyrate, an amino acid that is utilized as substrate in the reaction catalyzed by y-glutamylcysteine synthetase, led to a large accumulation of y-glutamyl-2-aminobutyrate and pyrrolidone carboxylate in mouse tissues. L-Methionine-RS-sulfoximine, an inhibitor of y-glutamylcysteine synthetase, abolished the increase in concentration of pyrrolidone carboxylate. No accumulation of pyrrolidone carboxylate was observed after L-cysteine. The separate administration of several protein amino acids had little effect on the concentration of pyrrolidone carboxylate ; however formation of small amounts of the corresponding y-glutamyl derivatives (e.g. y-glutamylmethionine and y-glutamylphenylalanine) was detected. These intermediates are probably formed by transpeptidation between glutathione and the corresponding amino acid, catalyzed by y-glutamyl transpeptidase. The concentration of pyrrolidone carboxylate increased significantly after administration of a mixture containing all protein amino acids, the highest increase occurring in the kidney.The results suggest that two separate pathways for the formation of y-glutamyl amino acids and pyrrolidone carboxylate exist in vivo. One of these results from the function of y-glutamylcysteine synthetase in glutathione synthesis. The other pathway involves the amino-acid-dependent degradation of glutathione, mediated by y-glutamyl transpeptidase. Only very small amounts of free intermediates are apparently derived from the latter pathway, suggesting that the y-glutamyl amino acids formed in this pathway are either enzyme-bound or are directly hydrolyzed to glutamate and free amino acid. y-glutamyl amino acids with the concomitant release of free amino acid. The enzyme is widely distributed in animal tissues [4] and is part of the y-glutamyl cycle which was proposed as a transport system for amino acids [5]. Further reactions of the cycle include: (a) conversion of L-pyrrolidone carboxylate to L-glutamate in an ATP-requiring reaction [6,7]; (b) the ATPdependent synthesis of glutathione catalyzed in sequence by y-glutamylcysteine synthetase and glutathione synthetase [8]; and (c) transfer of the y-glutamyl moiety of GSH to an amino acid to form the correEur. J. Biochem. 53 (1975)

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Section: Substratementioning

confidence: 99%

Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Orłowski

Wilk

1975

Eur J Biochem

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“…1, compound VI) might accumulate transiently in these strains. The ox-amino acid analog of compound VI, allylglycine, is highly toxic to a number of bacterial species, including E. coli (12). That deamination of allylglycine to 2-keto-4-pentenoic acid is involved in this toxicity is suggested by the observation that among mutants of E. coli isolated for their resistance to allylglycine, half had defects in D-alanine dehydrogenase (R. P. Burlingame, Ph.D. thesis, University of Minnesota, St. Paul, 1983), an enzyme of broad substrate and inducer specificity (14) that might be expected to carry out this deamination reaction.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation

Burlingame¹,

Wyman²,

Chapman³

1986

J Bacteriol

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Mutants of Escherichia coli defective in catabolism of 3-phenylpropionate, 3-(3-hydroxyphenyl)propionate, or both were isolated after mutagenesis with ethylmethane sulfonate. Nine phenotypically distinct classes of mutants were identified, including strains lacking each of the first five enzyme activities for the degradation of these compounds and mutants pleiotropically negative for some of these activities. Characterization of these mutants was greatly facilitated by the use of indicator media in which accumulation of 3-(2,3-dihydroxyphenyl)propionate or 2-hydroxy-6-ketononadienedioic acid led to the formation of dark red or bright yellow colors, respectively, in the medium. Assays with wild-type and mutant strains indicated that 3-phenylpropionate (or its dihydrodiol), but none of the hydroxylated derivatives tested, induced the synthesis of enzymes for its conversion to 3-(2,3-dihydroxyphenyl)propionate. The remaining enzymes were induced by the 2- or 3-hydroxy or 2,3-dihydroxy derivatives of 3-phenylpropionate, with the 2-hydroxy compound acting as an apparent gratuitous inducer. Metabolism to nonaromatic intermediates appeared to be unnecessary for full induction of any pathway enzyme. One unusual class of mutants, in which 2-keto-4-pentenoate hydratase appeared to be uninducible, indicated a level of control not previously shown in meta-fission catabolic pathways.

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“…It should also be noted that allylglycine was synthesized specifically to inhibit the divalent sulfur atom as found in cysteine (Dittmer et al, 1948). Assuming allylglycine enters the cultured cells, its inability to inhibit L-cystine in support of virus production and cell survival may indicate that cystine rather than cysteine is the active form of the amino acid in these processes.…”

Section: Discussionmentioning

confidence: 99%

l -CYSTINE REQUIREMENT FOR PRODUCTION OF COXSACKIE B3 VIRUS IN CULTURED MONKEY HEART CELLS

Tyndall

Ludwig

1963

J Bacteriol

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The requirement for L-cystine in both the production of Coxsackie B3 virus in cultured monkey heart cells and in prolonging the survival of the cultured monkey heart cells is demonstrated. D-Cystine, DL-homocystine, DL-allo-cystathionine, DL-homocysteine thiolactone, 2-mercaptoethlyamine, allylglycine, 3,3'-dithiopropionic acid, and DL-ethionine could not replace L-cystine in either supporting Coxsackie B3 virus production or prolonging monkey heart cell culture survival time. By their ineffectiveness, these compounds suggest the specificity of the L-cystine requirement. Allylglycine, 3, 3'-dithiopropionic acid, and DLethionine were likewise incapable of inhibiting the L-cystine effect in supporting both virus production and cell survival. Prolonged starvation of cell cultures prior to virus inoculation failed to reveal any additional marked nutritional requirements, but rather tended to accentuate the L-cystine requirement for virus production. Increased cell starvation did, however, lead to the establishment of a latent Coxsackie B3 virus infection of cultured monkey heart cells, the activation of which is L-cystinedependent. The requirement for the amino acid L-cystine (L-cysteine) in a variety of cell-virus systems has been previously demonstrated (Dubes, 1956; Rappaport, 1956; Tynidall and Ludwig, 1960). 1 Authorized for publication 25 January 1963 as paper no. 2470 in the journal series of the Pennsylvania Agricultural Experiment Station.

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The Inhibition of Microbiological Growth by Allylglycine, Methallylglycine and Crotylglycine^1,2

Cited by 28 publications

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Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation

l -CYSTINE REQUIREMENT FOR PRODUCTION OF COXSACKIE B3 VIRUS IN CULTURED MONKEY HEART CELLS

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The Inhibition of Microbiological Growth by Allylglycine, Methallylglycine and Crotylglycine1,2

Cited by 28 publications

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Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Intermediates of the gamma-Glutamyl Cycle in Mouse Tissues. Influence of Administration of Amino Acids on Pyrrolidone Carboxylate and gamma-Glutamyl Amino Acids

Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation

l -CYSTINE REQUIREMENT FOR PRODUCTION OF COXSACKIE B3 VIRUS IN CULTURED MONKEY HEART CELLS

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The Inhibition of Microbiological Growth by Allylglycine, Methallylglycine and Crotylglycine^1,2