Isolation and characterization of new phenolic siderophores with antimicrobial properties from Pseudomonas sp. UIAU-6B

• Emmanuel T. Oluwabusola,
• Olusoji O. Adebisi,
• Fernando Reyes,
• Kojo S. Acquah,
• Mercedes De La Cruz,
• Larry L. Mweetwa,
• Joy E. Rajakulendran,
• Digby F. Warner,
• Deng Hai,
• Rainer Ebel and
• Marcel Jaspars

Beilstein J. Org. Chem. 2021, 17, 2390–2398, doi:10.3762/bjoc.17.156

• Infectious Diseases Research in Africa, University of Cape Town, Rondebosch, 7701, South Africa 10.3762/bjoc.17.156 Abstract Five new phenolic siderophores 1–5 were isolated from the organic extract of a culture broth in a modified SGG medium of Pseudomonas sp. UIAU-6B, obtained from sediments collected

• ; pseudomonine; Pseudomonas sp.; vancomycin-sensitive Enterococcus faecium; Introduction The introduction of antimicrobial drugs in the mid-20th century has had an unprecedented positive impact on human health, but the current threat of multiple drug resistance may well roll back all these past achievements [1

• microbial sources led to the isolation of Pseudomonas sp. UIAU-6B from sediments collected from the Oyun river in North Central Nigeria. Herein, we report the isolation and structure elucidation of seven secondary metabolites including five new (1–5), and two known phenolic siderophores (6 and 7) [28][36

Identification of volatiles from six marine Celeribacter strains

• Anuj Kumar Chhalodia,
• Jan Rinkel,
• Dorota Konvalinkova,
• Jörn Petersen and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2021, 17, 420–430, doi:10.3762/bjoc.17.38

• from the roseobacter group is the production of the sulfur-containing antibiotic tropodithietic acid (TDA) in Phaeobacter piscinae DSM 103509T [28], a compound that is in equilibrium with its tautomer thiotropocin [29] that was first described from Pseudomonas sp. CB-104 [30]. Its biosynthesis depends

Syntheses of spliceostatins and thailanstatins: a review

• William A. Donaldson

Beilstein J. Org. Chem. 2020, 16, 1991–2006, doi:10.3762/bjoc.16.166

• (Figure 1) are a family of linear peptide/polyketide natural products isolated from the bacteria Burkholderia sp. FERM BP-3421 [1][2][3] (originally identified as Pseudomonas sp. No 2663) and Burkholderia sp. MSMB 43 [4][5]. These compounds are of interest due to their ability to bind to a subunit of the

Chemical structure of cichorinotoxin, a cyclic lipodepsipeptide that is produced by Pseudomonas cichorii and causes varnish spots on lettuce

• Hidekazu Komatsu,
• Takashi Shirakawa,
• Takeo Uchiyama and
• Tsutomu Hoshino

Beilstein J. Org. Chem. 2019, 15, 299–309, doi:10.3762/bjoc.15.27

• 22-B [13], corpeptin A and B [19], fuscopeptin [20] and tolaasin I [21][22], which are typical lipodepsipeptides produced by Pseudomonas sp., and they are structural analogues of cichorinotoxin. All of these peptides have a lipophilic fatty acid moiety connected to dhThr1-D-Pro2, and the amino acids

The enzymes of microbial nicotine metabolism

• Paul F. Fitzpatrick

Beilstein J. Org. Chem. 2018, 14, 2295–2307, doi:10.3762/bjoc.14.204

• NicA2 instead catalyzes oxidation of the substrate carbon–nitrogen bond as shown in Scheme 4. Cloning and expression of the protein encoded by the nox gene of Pseudomonas sp. HZN6 showed that it also catalyzes oxidation of nicotine to pseudooxynicotine [54]. The sequence of the protein is most similar

• enzyme as shown in Scheme 9, with the hydrolytic step being nonenzymatic. This is essentially the same reaction as that catalyzed by A. nicotinovorans γ-N-methylaminobutyrate demethylating oxidase (Mabo). E. coli expressing the sap gene from Pseudomonas sp. HZN6 will catalyze the NADP+-dependent

• converting 3-succinoylpyrimidine to 6-hydroxy-3-succinoylpyridine [48]. These results support the identification of SpmABC as a molybdopterin enzyme that catalyzes this step in the pathway. Enzymes with this activity do not appear to have been identified as yet for P. putida S5 and Pseudomonas sp. HZN6. HspA

Biosynthesis of α-pyrones

• Till F. Schäberle

Beilstein J. Org. Chem. 2016, 12, 571–588, doi:10.3762/bjoc.12.56

• moiety, was identified in Pseudomonas sp. GM30, and it was subsequently proven by heterologous expression experiments with ketosynthase which is responsible for the biosynthesis of these derivatives [63]. 1.3 Monobenzo-α-pyrones Synthetic derivatives of the natural product 4-hydroxycoumarin are widely

• dimerization is essential [63]. The pseudopyronine synthase PyrS represents a homologue of PpyS. Using PpyS from Pseudomonas sp. GM30, it was analyzed if this KS is also involved in the formation of α-pyrones. The two pseudopyronines A (55) and B (56) have been up to now isolated from different Pseudomonas

Natural products from microbes associated with insects

• Christine Beemelmanns,
• Huijuan Guo,
• Maja Rischer and
• Michael Poulsen

Beilstein J. Org. Chem. 2016, 12, 314–327, doi:10.3762/bjoc.12.34

• potent toxin that can ward of natural predators such as wolf spiders [48]. The initial isolation of pederin (3) included the collection and chemical analysis of 250,000 beetles. Later, the true producer was found to be an endosymbiotic Pseudomonas sp. within the female beetle which was identified by

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

• Barış Binay,
• Dilek Alagöz,
• Deniz Yildirim,
• Ayhan Çelik and
• S. Seyhan Tükel

Beilstein J. Org. Chem. 2016, 12, 271–277, doi:10.3762/bjoc.12.29

• ] reported the optimal pH values were 7.0 for both free FDH and immobilized FDH onto polydopamine-coated iron oxide nanoparticles (PD-IONPs). The optimum pH values of the both free Pseudomonas sp. 101 FDH and its immobilized form onto glyoxylagarose were reported as 7.0 [16]. The temperature–activity

A novel and widespread class of ketosynthase is responsible for the head-to-head condensation of two acyl moieties in bacterial pyrone biosynthesis

• Darko Kresovic,
• Florence Schempp,
• Zakaria Cheikh-Ali and
• Helge B. Bode

Beilstein J. Org. Chem. 2015, 11, 1412–1417, doi:10.3762/bjoc.11.152

• mechanism of pyrone formation has been investigated by amino acid exchange and bioinformatic analysis. Additionally, the evolutionary origin of PpyS has been studied by phylogenetic analyses also revealing homologous enzymes in Pseudomonas sp. GM30 responsible for the biosynthesis of pseudopyronines

• with OleA. As expected, the remaining 51 sequences show a higher similarity to PpyS and the newly formed PpyS branch shows a separation into two distinct groups with PpyS and PyrS (pseudopyronine synthase) being present in one of them. The homologue PyrS from Pseudomonas sp. GM30 is described below

• pyrone biosynthesis we analyzed the KS from Pseudomonas sp. GM30, as we knew that α-pyrone antibiotics pseudopyronine A (9) and B (10) have been isolated in two Pseudomonas strains but neither their biosynthesis nor the involved KS had been reported yet [28]. Both compounds have been described to show an

Biosynthesis of rare hexoses using microorganisms and related enzymes

• Zijie Li,
• Yahui Gao,
• Hideki Nakanishi,
• Xiaodong Gao and
• Li Cai

Beilstein J. Org. Chem. 2013, 9, 2434–2445, doi:10.3762/bjoc.9.281

• characterized the DTEase from Pseudomonas sp. ST-24 [28] and utilized this enzyme in the mass production of D-psicose with a final concentration of 150 g/L [29]. They further packed the immobilized DTEase from Pseudomonas sp. ST-24 (on Chitopearl beads) into a column that could be continuously used for 10 days

• galactitol catalyzed by Pseudomonas sp. ST 24 and the production yield was as high as 70%. The possible transformation route from galactitol to D-sorbose in this strain was deduced as follows (Scheme 4): the substrate galactitol is dehydrogenated at C-2 to afford D-tagatose followed by C-3 epimerization [43

• ]. Izumori et al. established a method for the preparation of D-sorbose directly from D-tagatose with immobilized DTEase from Pseudomonas sp. ST-24 and 2 g of D-sorbose could be obtained from 3 g of D-tagatose. The conversion yield maintained at about 70% each time even if the batch was repeated five times

Identification and isolation of insecticidal oxazoles from Pseudomonas spp.

• Florian Grundmann,
• Veronika Dill,
• Andrea Dowling,
• Aunchalee Thanwisai,
• Edna Bode,
• Narisara Chantratita,
• Richard ffrench-Constant and
• Helge B. Bode

Beilstein J. Org. Chem. 2012, 8, 749–752, doi:10.3762/bjoc.8.85

• its 16S-rRNA gene revealing it to be a Pseudomonas sp. with closest homology to P. putida (100% similarity: Supporting Information File 1, Figure S4) [11][12][13][14]. As judged on the basis of high-resolution MALDI–MS and LC–ESIMS/MS data the well-known entomopathogenic P. entomophila [15][16] also

Mutational analysis of a phenazine biosynthetic gene cluster in Streptomyces anulatus 9663

• Orwah Saleh,
• Katrin Flinspach,
• Lucia Westrich,
• Andreas Kulik,
• Bertolt Gust,
• Hans-Peter Fiedler and
• Lutz Heide

Beilstein J. Org. Chem. 2012, 8, 501–513, doi:10.3762/bjoc.8.57

• ]. The LysR-like protein PqsR from Pseudomonas sp. M18 is involved in the regulation of phenazine biosynthesis. Inactivation of pqsR resulted in almost complete abolishment of the transcription of the phenazine biosynthesis genes [21]. It may therefore be speculated that ppzY codes for a positive

Coupled chemo(enzymatic) reactions in continuous flow

• Ruslan Yuryev,
• Simon Strompen and
• Andreas Liese

Beilstein J. Org. Chem. 2011, 7, 1449–1467, doi:10.3762/bjoc.7.169

• biofilm membrane reactor (Scheme 24) [52][53]. Cells of Pseudomonas sp. were grown in a biofilm attached to the inner surface of a silicon tube, through which a nutrient solution was constantly pumped. In a specially designed hermetic reaction compartment the tube was partially submerged into liquid 73

• Pseudomonas sp. [53]. Reduction of estrone (75) to β-estradiol (76) by Saccharomyces cerevisiae in a cascade of two stirred-tank reactors [54]. Advantages and disadvantages of the three approaches to continuous coupled-reaction (chemo)enzymatic processes.a

Recent progress on the total synthesis of acetogenins from Annonaceae

• Nianguang Li,
• Zhihao Shi,
• Yuping Tang,
• Jianwei Chen and
• Xiang Li

Beilstein J. Org. Chem. 2008, 4, No. 48, doi:10.3762/bjoc.4.48