137. Chemistry of micrococcin P. Part I

Brookes, P. C.; Fuller, A. T.; Walker, James

doi:10.1039/jr9570000689

Cited by 51 publications

(29 citation statements)

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“…3) is a macrocyclic peptide antibiotic of the thiocillin-thiazolyl class (8,9,13,25,32,54). Recently, a complete synthesis was published by Okumura et al (34).…”

Section: Discussionmentioning

confidence: 99%

“…By screening the surface ripening flora of German and French smeared cheeses with respect to their antilisterial potential, the highly inhibitory Staphylococcus equorum was isolated from the surface of a traditional French Raclette cheese, where it was found in cell numbers up to 10 8 per cm 2 (the present study). The genus Staphylococcus is known to produce many antibacterial substances (41,42).…”

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confidence: 99%

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The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

Carnio

Höltzel

Rudolf

et al. 2000

Appl Environ Microbiol

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Staphylococcus equorum WS 2733 was found to produce a substance exhibiting a bacteriostatic effect on a variety of gram-positive bacteria. The metabolite was purified to homogeneity by ammonium sulfate precipitation and semipreparative reversed-phase high-performance liquid chromatography. Electrospray mass spectrometry confirmed the high purity of the compound and revealed a molecular mass of 1,143 Da. By twodimensional nuclear magnetic resonance spectroscopy the substance was identified as micrococcin P 1 which is a macrocyclic peptide antibiotic that has not yet been reported for the genus Staphylococcus. A total of 95 out of 95 Listeria strains and 130 out of 135 other gram-positive bacteria were inhibited by this substance, while none of 37 gram-negative bacteria were affected. The antilisterial potential of this food-grade strain as a protective starter culture was evaluated by its in situ application in cheese-ripening experiments under laboratory conditions. A remarkable growth reduction of Listeria monocytogenes could be achieved compared to control cheese ripened with a nonbacteriocinogenic type strain of Staphylococcus equorum. In order to prove that inhibition was due to micrococcin P 1 , a micrococcin-deficient mutant was constructed which did not inhibit L. monocytogenes in cheese-ripening experiments.

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“…3) is a macrocyclic peptide antibiotic of the thiocillin-thiazolyl class (8,9,13,25,32,54). Recently, a complete synthesis was published by Okumura et al (34).…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

Carnio

Höltzel

Rudolf

et al. 2000

Appl Environ Microbiol

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“…Thiamine was found as the first natural com pound containing a thiazole ring. Recently, the presence of the thiazole ring system has been demonstrated in luciferin (11) and in antibiotics, such as micrococcin P (12,13), bottromycin (14), thiostrepton (15,16), and bacitracin F (17). Chemical structure similar to the thiazole ring system has been found in bacitracin A (18).…”

mentioning

confidence: 99%

“…Under the presence of a large amount of cysteine in a medium, the thiamine content per unit weight of cells is high but the growth of Escherichia coli is strongly inhibited. It was already indicated that antibiotics containing thiazole ring such as micrococcin P (12,13), bottromycin (14), thiostrepton (15,16), and bacitracin F (17) were synthesized from polypeptide containing cysteine. Moreover, it was shown that luciferin (11) isolated from the firefly contained both benzothiazole and thiazolidine rings.…”

Section: Table II Effect Of Amino Acids On the Productionmentioning

confidence: 99%

Effect of Sulfur-Containing Amino Acids on the Production of Thiamine by Escherichia Coli

Akagi¹,

Kumaoka²

1963

J. Vitaminol

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It has now been firmly established by several groups of workers (1-10) that in yeast thiamine is enzymatically synthesized from pyrimidine pyrophosphate and thiazole monophosphate.However, there is little information about the biosynthetic pathways of pyrimidine and thiazole themselves. Thiamine was found as the first natural com pound containing a thiazole ring. Recently, the presence of the thiazole ring system has been demonstrated in luciferin (11) and in antibiotics, such as micrococcin P (12, 13), bottromycin (14), thiostrepton (15, 16), and bacitracin F (17). Chemical structure similar to the thiazole ring system has been found in bacitracin A (18). It was indicated clearly that they were derived from polypeptides containing cysteine and by cyclization to a thiazoline for bacitracin A and by cyclization followed by de hydrogenation to thiazole rings for the others. The chemical structure of penicillin in which the thiazolidine ring is a dipeptide composed of a cysteine derivative and valine. It has been established that C14-, S35-, and H3-labelled cysteine gave rise to labelled penicillin (19)(20)(21).It is considered that the thiazole ring of thiamine is also syn thesized via sulfur-containing amino acid. Such concepts were already presented by several workers without reliable data (22)(23)(24)(25).A detailed study was made on the effect of sulfur-containing amino acids and other amino acids on the production of thiamine by Escherichia coli. EXPERIMENTAL

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“…Even now some structural uncertainties remain, no more so than in the case of micrococcin itself, the first thiopeptide to be isolated in 1948, and one of the first to attract the attention of synthetic organic chemists. The structure of a substance known as micrococcin P was first investigated by Walker and co-workers, [18][19][20][21][22] but following the discovery that micrococcin P was actually a mixture of two compounds, micrococcins P1 and P2, it was Bycroft and Gowland who assigned micrococcin P1 as structure 1 a. [23] (The proposal outlined in Ref.…”

Section: Introductionmentioning

confidence: 98%

From Amino Acids to Heteroaromatics—Thiopeptide Antibiotics, Nature's Heterocyclic Peptides

2007

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Amino acids, the building blocks of proteins, also serve as precursors to a wide range of other naturally occurring substances including alkaloids, antibiotics, and, the subject of this Review, heterocyclic peptides. Simple alpha-amino acids are converted into complex arrays of heteroaromatic rings that display interesting and potent biological activity. The thiopeptide antibiotics, with their complex molecular architectures, are wonderful examples. In this Review we show how organic chemists have developed innovative methods for the synthesis of the heterocyclic ring systems, including routes inspired by the likely biosynthetic processes, and successfully assembled such building blocks into the final target molecule by application of orthogonal protecting groups and coupling methodologies.

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137. Chemistry of micrococcin P. Part I

Cited by 51 publications

References 0 publications

The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

Effect of Sulfur-Containing Amino Acids on the Production of Thiamine by Escherichia Coli

From Amino Acids to Heteroaromatics—Thiopeptide Antibiotics, Nature's Heterocyclic Peptides

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137. Chemistry of micrococcin P. Part I

Cited by 51 publications

References 0 publications

The Macrocyclic Peptide Antibiotic Micrococcin P1Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

The Macrocyclic Peptide Antibiotic Micrococcin P1Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

Effect of Sulfur-Containing Amino Acids on the Production of Thiamine by Escherichia Coli

From Amino Acids to Heteroaromatics—Thiopeptide Antibiotics, Nature's Heterocyclic Peptides

Contact Info

Product

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The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese

The Macrocyclic Peptide Antibiotic Micrococcin P₁Is Secreted by the Food-Borne BacteriumStaphylococcus equorumWS 2733 and InhibitsListeria monocytogeneson Soft Cheese