Biosynthesis of Rhizocticins, Antifungal Phosphonate Oligopeptides Produced by Bacillus subtilis ATCC6633

Borisova, Svetlana A.; Circello, Benjamin T.; Zhang, Jun Kai; Donk, Wilfred A. van der; Metcalf, William W.

doi:10.1016/j.chembiol.2009.11.017

Cited by 99 publications

(103 citation statements)

References 56 publications

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“…Bacillaene, difficidin and macrolactin are polyketides displaying a broad spectrum of antibacterial activities that may be involved in the biocontrol activity of the producing strain such as in the case of fire blight, a serious disease of orchard trees caused by Erwinia amylovora ). The phosphono-oligopeptide rhizocticin produced by B. subtilis also displays antifungal and nematicidal activities, but does not retain any bactericidal properties (Borisova et al, 2010). Peptide compounds represent the predominant class of Bacillus antibiotics.…”

Section: Direct Inhibition Of Phytopathogens 421 Antibiosis Membersmentioning

confidence: 99%

Bacillus-Based Biological Control of Plant Diseases

Cawoy

Bettiol²,

Fickers

et al. 2011

Pesticides in the Modern World - Pesticides Use and Management

150

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Section: Direct Inhibition Of Phytopathogens 421 Antibiosis Membersmentioning

confidence: 99%

Bacillus-Based Biological Control of Plant Diseases

Cawoy

Bettiol²,

Fickers

et al. 2011

Pesticides in the Modern World - Pesticides Use and Management

150

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“…acute cystitis; FR-900098 and fosmidomycin, antimicrobials undergoing clinical trials for malaria; and phosphinothricin, the active component in several commercial herbicides (Liberty, Basta, and Rely). Second, the methodology needed for gene-based discovery of phosphonate biosynthetic loci has been rigorously established (17)(18)(19)(20)(21)(22)(23). This method relies on the fact that all but two characterized phosphonate biosynthetic pathways begin with the enzyme phosphoenolpyruvate (PEP) mutase (encoded by pepM) (14).…”

Section: Significancementioning

confidence: 99%

Discovery of phosphonic acid natural products by mining the genomes of 10,000 actinomycetes

Gao

Doroghazi

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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189

185

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Although natural products have been a particularly rich source of human medicines, activity-based screening results in a very high rate of rediscovery of known molecules. Based on the large number of natural product biosynthetic genes in microbial genomes, many have proposed "genome mining" as an alternative approach for discovery efforts; however, this idea has yet to be performed experimentally on a large scale. Here, we demonstrate the feasibility of large-scale, high-throughput genome mining by screening a collection of over 10,000 actinomycetes for the genetic potential to make phosphonic acids, a class of natural products with diverse and useful bioactivities. Genome sequencing identified a diverse collection of phosphonate biosynthetic gene clusters within 278 strains. These clusters were classified into 64 distinct groups, of which 55 are likely to direct the synthesis of unknown compounds. Characterization of strains within five of these groups resulted in the discovery of a new archetypical pathway for phosphonate biosynthesis, the first (to our knowledge) dedicated pathway for H-phosphinates, and 11 previously undescribed phosphonic acid natural products. Among these compounds are argolaphos, a broad-spectrum antibacterial phosphonopeptide composed of aminomethylphosphonate in peptide linkage to a rare amino acid N 5 -hydroxyarginine; valinophos, an N-acetyl L-Val ester of 2,3-dihydroxypropylphosphonate; and phosphonocystoximate, an unusual thiohydroximate-containing molecule representing a new chemotype of sulfur-containing phosphonate natural products. Analysis of the genome sequences from the remaining strains suggests that the majority of the phosphonate biosynthetic repertoire of Actinobacteria has been captured at the gene level. This dereplicated strain collection now provides a reservoir of numerous, as yet undiscovered, phosphonate natural products.natural products | genome mining | phosphonic acid | antibiotic

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“…However, there are more reports on the biosynthesis of peptidic secondary metabolites involving nonribosomal peptide synthetase than reports describing Lals (26). Rhizocticin and phaseolotoxin are di-or tripeptide antibiotic and tripeptide phytotoxins, respectively, that contain an unusual amino acid, and two ATP-grasp enzymes were identified in each biosynthetic gene cluster (27,28). In rhizocticin biosynthesis, our results revealed that two Lals (RizA and RizB) combined three amino acids, yielding tripeptides similar to rhizocticin (19,20).…”

mentioning

confidence: 70%

l -Amino Acid Ligase from Pseudomonas syringae Producing Tabtoxin Can Be Used for Enzymatic Synthesis of Various Functional Peptides

Arai

Arimura

Ishikura

et al. 2013

Appl Environ Microbiol

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Functional peptides are expected to be beneficial compounds that improve our quality of life. To address the growing need for functional peptides, we have examined peptide synthesis by using microbial enzymes. L-Amino acid ligase (Lal) catalyzes the condensation of unprotected amino acids in an ATP-dependent manner and is applicable to fermentative production. Hence, Lal is a promising enzyme to achieve cost-effective synthesis. To obtain a Lal with novel substrate specificity, we focused on the putative Lal involved in the biosynthesis of the dipeptidic phytotoxin designated tabtoxin. The tabS gene was cloned from Pseudomonas syringae NBRC14081 and overexpressed in Escherichia coli cells. The recombinant TabS protein produced showed the broadest substrate specificity of any known Lal; it detected 136 of 231 combinations of amino acid substrates when dipeptide synthesis was examined. In addition, some new substrate specificities were identified and unusual amino acids, e.g., L-pipecolic acid, hydroxy-L-proline, and ␤-alanine, were found to be acceptable substrates. Furthermore, kinetic analysis and monitoring of the reactions over a short time revealed that TabS showed distinct substrate selectivity at the N and C termini, which made it possible to specifically synthesize a peptide without by-products such as homopeptides and heteropeptides with the reverse sequence. TabS specifically synthesized the following functional peptides, including their precursors: L-arginyl-L-phenylalanine (antihypertensive effect; yield, 62%), L-leucyl-L-isoleucine (antidepressive effect; yield, 77%), L-glutaminyl-L-tryptophan (precursor of L-glutamyl-L-tryptophan, which has antiangiogenic activity; yield, 54%), L-leucyl-L-serine (enhances saltiness; yield, 83%), and L-glutaminyl-L-threonine (precursor of L-glutamyl-L-threonine, which enhances saltiness; yield, 96%). Furthermore, our results also provide new insights into tabtoxin biosynthesis.

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Biosynthesis of Rhizocticins, Antifungal Phosphonate Oligopeptides Produced by Bacillus subtilis ATCC6633

Cited by 99 publications

References 56 publications

Bacillus-Based Biological Control of Plant Diseases

Bacillus-Based Biological Control of Plant Diseases

Discovery of phosphonic acid natural products by mining the genomes of 10,000 actinomycetes

l -Amino Acid Ligase from Pseudomonas syringae Producing Tabtoxin Can Be Used for Enzymatic Synthesis of Various Functional Peptides

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