Biosynthesis of thiopeptide antibiotic A10255: Incorporation of isotopically-labeled precursors.

Favret, Montgomery E.; Paschal, Jonathan W.; Elzey, Thomas K.; Boeck, L. D.

doi:10.7164/antibiotics.45.1499

Cited by 22 publications

(20 citation statements)

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“…The impossibility to obtain crystals for the vast majority of them prompted the assignment of their structure without a clear evidence of their stereochemistry. In spite of this limitation, in many cases their configuration has been proposed by analogy with similar isolates [38,39], via amino acid analysis [40,41,42] or via isotopic labeling through feeding with labeled amino acids [43,44]. In some cases, less conventional techniques have been chosen.…”

Section: Thiopeptidesmentioning

confidence: 99%

Thiopeptide Antibiotics: Retrospective and Recent Advances

2014

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Thiopeptides, or thiazolyl peptides, are a relatively new family of antibiotics that already counts with more than one hundred different entities. Although they are mainly isolated from soil bacteria, during the last decade, new members have been isolated from marine samples. Far from being limited to their innate antibacterial activity, thiopeptides have been found to possess a wide range of biological properties, including anticancer, antiplasmodial, immunosuppressive, etc. In spite of their ribosomal origin, these highly posttranslationally processed peptides have posed a fascinating synthetic challenge, prompting the development of various methodologies and strategies. Regardless of their limited solubility, intensive investigations are bringing thiopeptide derivatives closer to the clinic, where they are likely to show their veritable therapeutic potential.

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Section: Thiopeptidesmentioning

confidence: 99%

Thiopeptide Antibiotics: Retrospective and Recent Advances

2014

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“…There is precedence for thiazole ring formation from Cys in bacteria (Favret et al, 1992). Microcin B17 is a member of a group of low-molecular-weight polypeptide antibiotics produced by many different species of enteric bacteria (Genilloud et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Origin of the Thiazole Ring of Camalexin, a Phytoalexin from Arabidopsis thaliana

Zook

Hammerschmidt

1997

Plant Physiology

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The principal phytoalexin that accumulates i n Arabidopsis fbaliana after infection by fungi or bacteria is 3-thiazol-2'-yl-indole (camalexin). Many plant species produce antimicrobial compounds, known as phytoalexins, after pathogen infection. In general, members of a particular plant family will produce phytoalexins that belong to the same class of compounds (Bailey and Mansfield, 1982). Leguminous plants produce isoflavanoid and/ or pterocarpan phytoalexins, whereas solanaceous plants produce sesquiterpenoid phytoalexins. AI1 of the phytoalexins that have been characterized from the members of the Brassicaceae are indole derivatives that are substituted at the C-3 position with a sulfur-containing moiety (Hammerschmidt et al., 1993). Conn et al. (1988) reported that Cumelina sativa (false flax) accumulated two different phytoalexins after infection with Alternaria brassicae, a funga1 pathogen of rapeseed. The most abundant of the two phytoalexins was identified

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“…1). Inspired by the amino acid supplementation experiment of this study, glycine, serine and threonine were suggested to be the limiting precursors for the biosynthesis of apramycin similar to the cases where certain amino acids were able to contribute to the biosynthesis of antibiotics as the "building units" or precursors [18][19][20][21] . The subsequent [2-13 C]glycine and [2-13 C, 15 N]serine incorporation experiments revealed that the only methyl group of apramycin on C7′-N of the octodiose was derived from the C2 of glycine while serine might contribute to the substituents of -NH 2 .…”

Section: Discussionmentioning

confidence: 97%

Glycine origin of the methyl substituent on C7′-N of octodiose for the biosynthesis of apramycin

Zhu

Zhikun

et al. 2006

SCI CHINA SER C

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Apramycin is unique in the aminoglycoside family due to its octodiose moiety. However, either the biosynthesis process or the precursors involved are largely unknown. Addition of glycine, as well as serine or threonine, to the Streptomyces tenebrabrius UD2 fermentation medium substantially increases the production of apramycin with little effect on the growth of mycelia, indicating that glycine and/or serine might be involved in the biosynthesis of apramycin. The 13C-NMR analysis of [2-13C] glycine-fed (25% enrichment) apramycin showed that glycine specifically and efficiently incorporated into the only N-CH3 substituent of apramycin on the C7' of the octodiose moiety. We noticed that the in vivo concentration of S-adenosyl methionine increased in parallel with the addition of glycine, while the addition of methione in the fermentation medium significantly decreased the productivity of apramycin. Therefore, the methyl donor function of glycine is proposed to be involved in the methionine cycle but methionine itself was proposed to inhibit the methylation and methyl transfer processes a previously reported for the case of rapamycin. The 15N NMR spectra of [2-13C,15N]serine labeled apramycin indicated that serine may also act as a limiting precursor contributing to the -NH2 substituents of apramycin.

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Biosynthesis of thiopeptide antibiotic A10255: Incorporation of isotopically-labeled precursors.

Cited by 22 publications

References 0 publications

Thiopeptide Antibiotics: Retrospective and Recent Advances

Thiopeptide Antibiotics: Retrospective and Recent Advances

Origin of the Thiazole Ring of Camalexin, a Phytoalexin from Arabidopsis thaliana

Glycine origin of the methyl substituent on C7′-N of octodiose for the biosynthesis of apramycin

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