Investigations on the mode of action of cyclo-serine upon protein synthesis in Escherichia coli

Barbieri, Paola; Marco, A. Di; Fuoco, L; Rusconi, A.

doi:10.1016/0006-2952(60)90026-5

Cited by 11 publications

(3 citation statements)

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“…It was suggested by Park (1958) that the antibiotic is a structural analog of D-alanine and might "prevent the normal incorporation of D-alanine into the wall." Barbieri et al (1960) demonstrated that D-cycloserine inhibits the incorporation of dlalanine-l-14C into the cell wall and protein fractions of Escherichia coli.…”

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The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*

Neuhaus¹,

Lynch²

1964

Biochemistry

186

160

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The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*

Neuhaus¹,

Lynch²

1964

Biochemistry

186

160

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“…In contrast to the results with D-cycloserine, growth of S. aureus in the presence of L-cycloserine does not result in the accumulation of UDPNAc-amino sugar (CIAK and HAHN, 1959). In E. coli, BARBIERI et al (1960) demonstrated that D-cycloserine inhibits the incorporation of DL-alanine-1-[1 4 C] into the cell wall and to a lesser extent into the protein fraction.The structure of the UDP-NAc-amino sugar which accumulates in the presence of D-cycloserine was elucidated by STROMINGER, THRENN, and SCOTT (1959) and found to be: In 5. aureus, the accumulation of this nucleotide was reversed by the addition of D-alanine to the medium. L-Alanine, DL-alanyl-DL-alanine, and D-serine at high concentrations were not effective (STROMINGER, THRENN, and ScoTT, 1959 n-ala were effective in reversing the nucleotide accumulation induced by n-cycloserine (3 X 10-4 M) in S. aureus Copenhagen.…”

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Antibiotics

1967

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AII rights, especially that of tnmslation into foreign languages, reserved. It is also forbidden to reproduce this book, either whole DedicationFor most areas of scientific pursuit, there is usually that rare investigator who has the imagination to conceive ideas, who has faith in his visions, and who has the ability to critically test his concepts in the laboratory. Almost invariably, this scientist also inspires younger men to enthusiastically enter into his research program. To him should go the accolades and the recognitions of the esteem in which he is held. As only a small part of this esteem, we wish to dedicate these books to Professor SELMAN A. W AKSMAN in appreciation of his leadership and contributions in all facets of antibiotic research. PrefaceThe idea for publishing these books on the mechanism of action and on the biosynthesis of antibiotics was born of frustration in our attempts to keep abreast of the literature. Gone were the years when we were able to keep a bibliography on antibiotics and feel confident that we could find everything that was being published on this subject. These fields of investigation were moving forward so rapidly and were encompassing so wide a range of specialized areas in microbiology and chemistry that it was almost impossible to keep abreast of developments. In our naivete and enthusiasm, however, we were unaware that we were toying with an idea that might enmesh us, that we were creating an entity with a life of its own, that we were letting loose a Golom who instead of being our servant would be our master.That we set up ideals for these books is obvious; they would be current guides to developments and information in the areas of mechanism of action and biosynthesis of antibiotics. For almost every subject, we wished to enlist the aid of an investigator who himself had played a part in determining the nature of the phenomena that were being discussed. One concept for the books was that they include only antibiotics for which a definitive, well-documented mechanism of action or biosynthetic pathway was known. Yet, such an approach would not entirely serve the purpose we projected, for it would not encompass all of the information available in these fields of antibiotic investigations and blind searches for the original literature would still have to be made. We therefore chose to include any and all antibiotics about which some pertinent information had been published. It was obvious even at the start that such a compilation, integration, and analysis of information could never be complete unless scientific investigations ceased at the moment the last manuscript was submitted-an end that was neither desirable nor possible. An addendum was therefore included at the end of the volume and left open for the addition of new information until the last pages of the regular articles had been printed.The original concept has also been further expanded as the authors of several papers found it advisable to elaborate on their subject. Some of the articles included discussions...

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“…It is unlikely, however, that they use the reverse of these synthetic routes for the degradation of D-amino acids, for the cells contain a D-amino acid oxidase (7,20,21). Although it has long been assumed that D-amino acids are degraded directly, rather than by conversion to their L enantiomers, only recently has it been suggested that some L-amino acids in bacteria might be degraded indirectly by conversion first to their D enantiomers (1,6,19,24).…”

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d -Alanine Oxidase from Escherichia coli : Participation in the Oxidation of l -Alanine

1973

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Cell wall-membrane preparations of Escherichia coli, prepared by the ethylenediaminetetraacetic acid-lysozyme method, contain enzymes which catalyze the oxidation of D-alanine and, to a lesser extent, L-alanine into pyruvate and ammonia without the formation of hydrogen peroxide. The kinetic parameters were (i) pH optima of 8.3 to 8.4 for Land D-alanine and (ii) a Km value of 6.6 i 0.2 mM for D-alanine. Several coenzymes were without effect when added to the reaction mixture. The participation of D-alanine oxidase in the oxidation of L-alanine was demonstrated. The evidence is based on (i) results of cellular fractionation; (ii) labeling experiments; (iii) inhibition studies with aminooxyacetate and cycloserine; (iv) denaturation experiments; and (v) demonstration of the presence of an active racemase.

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Investigations on the mode of action of cyclo-serine upon protein synthesis in Escherichia coli

Cited by 11 publications

References 3 publications

The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*

The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*

Antibiotics

d -Alanine Oxidase from Escherichia coli : Participation in the Oxidation of l -Alanine

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Investigations on the mode of action of cyclo-serine upon protein synthesis in Escherichia coli

Cited by 11 publications

References 3 publications

The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine*

The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine*

Antibiotics

d -Alanine Oxidase from Escherichia coli : Participation in the Oxidation of l -Alanine

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The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*

The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine^*