Enterobactin and Enantioenterobactin

Marinez, Eric R.; Salmassian, Eric K.; Lau, Thomas T.; Gutiérrez, Carlos Gutièrrez

doi:10.1021/jo9520194

Cited by 31 publications

(30 citation statements)

References 21 publications

(29 reference statements)

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“…5a was reacted, again under Yamaguchi esterification conditions, with 10 to give, in 90% yield, the diprotected linear dimer 11. Linear dimer 13 was prepared by di-deprotection of 11 in two steps using TBAF/THF (yields (12) in 81%) and Pd(PPh 3 ) 4 /morpholine/THF 31 (yields (13) in 99% yield). Linear trimer 17 was obtained by reacting the monoprotected dimer 12 with the monomer acid unit 5a under Yamaguchi conditions to give the diprotected linear trimer 15.…”

Section: Resultsmentioning

confidence: 99%

“…Thermodynamic translactonization has been used intramolecularly by Corey for the synthesis of medium ring monocyclic lactones, 8 by several groups intermolecularly for the cyclizations of -alkanolactones, 9,10 where the ring-size distributions give good agreement with theoretical expectations, 11 as well as the synthesis of a few natural products such as Enterobactin. 12 The chemistry we envisaged for thermodynamic cyclization of large building blocks is straightforward:…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Macrocycles Derived from Cinchona Alkaloids: A Thermodynamic vs Kinetic Study

Rowan

Sanders

1998

J. Org. Chem.

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Cyclization of the quinine-derived monomer (2a): HO-Cq-OMe, under thermodynamic control, gives mainly cyclic trimer Cq 3 (7a), whereas kinetic cyclization of the similar monomer HO-Cq-OH (8) gives a mixture of cyclic products. This difference in product distribution is attributed to predisposition of the monomer unit, which means the building block adopts a more stable conformation in cyclic trimer than it can in cyclic tetramer. The reversibility of the thermodynamic reaction was demonstrated using electrospray mass spectrometry to monitor the catalyzed mixing of the two cyclic trimers Cq 3 (7a) and Cc 3 (7b), which results in the statistically expected 1:3:3:1 ratio of all possible cyclic trimers Cc 3 :Cc 2 Cq:CcCq 2 :Cq 3 .

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Macrocycles Derived from Cinchona Alkaloids: A Thermodynamic vs Kinetic Study

Rowan

Sanders

1998

J. Org. Chem.

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“…Siderophore synthesis. Enterobactin, MECAM, DBS monomer, fluvibactin, fluvibactin A, vibriobactin, and vibriobactin A were synthesized as previously published (30)(31)(32)(33). The synthesis of DBS dimers and DBS trimers is reported in the supplemental material.…”

Section: Methodsmentioning

confidence: 99%

Catechol Siderophore Transport by Vibrio cholerae

et al. 2015

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Siderophores, small iron-binding molecules secreted by many microbial species, capture environmental iron for transport back into the cell. Vibrio cholerae synthesizes and uses the catechol siderophore vibriobactin and also uses siderophores secreted by other species, including enterobactin produced by Escherichia coli. E. coli secretes both canonical cyclic enterobactin and linear enterobactin derivatives likely derived from its cleavage by the enterobactin esterase Fes. We show here that V. cholerae does not use cyclic enterobactin but instead uses its linear derivatives. V. cholerae lacked both a receptor for efficient transport of cyclic enterobactin and enterobactin esterase to promote removal of iron from the ferrisiderophore complex. To further characterize the transport of catechol siderophores, we show that the linear enterobactin derivatives were transported into V. cholerae by either of the catechol siderophore receptors IrgA and VctA, which also transported the synthetic siderophore MECAM [1,3,5-N,N=,N؆-tris-(2,3-dihydroxybenzoyl)-triaminomethylbenzene]. Vibriobactin is transported via the additional catechol siderophore receptor ViuA, while the Vibrio fluvialis siderophore fluvibactin was transported by all three catechol receptors. ViuB, a putative V. cholerae siderophore-interacting protein (SIP), functionally substituted for the E. coli ferric reductase YqjH, which promotes the release of iron from the siderophore in the bacterial cytoplasm. In V. cholerae, ViuB was required for the use of vibriobactin but was not required for the use of MECAM, fluvibactin, ferrichrome, or the linear derivatives of enterobactin. This suggests the presence of another protein in V. cholerae capable of promoting the release of iron from these siderophores. IMPORTANCEVibrio cholerae is a major human pathogen and also serves as a model for the Vibrionaceae, which include other serious human and fish pathogens. The ability of these species to persist and acquire essential nutrients, including iron, in the environment is epidemiologically important but not well understood. In this work, we characterize the ability of V. cholerae to acquire iron by using siderophores produced by other organisms. We resolve confusion in the literature regarding its ability to use the Escherichia coli siderophore enterobactin and identify the receptor and TonB system used for the transport of several siderophores. The use of some siderophores did not require the ferric reductase ViuB, suggesting that an uncharacterized ferric reductase is present in V. cholerae.

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“…27 Deprotection of β-lactone derivatives 3a 27 and 3b with trifluoroacetic acid in the presence of p -toluensulfonic acid gave the tosylate salts ( S )- and ( R )-2-oxo-3-oxetanylammonium toluene-4-sulfonate ( 4a 28 and 4b 29), respectively 28,29. Alternatively, 4a can be obtained from the commercially available ( S )-3-(tritylamino)oxetan-2-one (Scheme 1).…”

Section: Chemistrymentioning

confidence: 99%

Synthesis and Structure−Activity Relationships of N-(2-Oxo-3-oxetanyl)amides as N-Acylethanolamine-hydrolyzing Acid Amidase Inhibitors

et al. 2010

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The fatty acid ethanolamides (FAEs) are a family of bioactive lipid mediators that include the endogenous agonist of peroxisome proliferator-activated receptor-α, palmitoylethanolamide (PEA). FAEs are hydrolyzed intracellularly by either fatty acid amide hydrolase or N-acylethanolamine-hydrolyzing acid amidase (NAAA). Selective inhibition of NAAA by (S)-N-(2-oxo-3-oxetanyl)-3-phenylpropionamide [(S)-OOPP, 7a] prevents PEA degradation in mouse leukocytes and attenuates responses to proinflammatory stimuli. Starting from the structure of 7a a series of β-lactones was prepared and tested on recombinant rat NAAA to explore structure-activity relationships (SARs) for this class of inhibitors and improve their in vitro potency. Following the hypothesis that these compounds inhibit NAAA by acylation of the catalytic cysteine, we identified several requirements for recognition at the active site and obtained new potent inhibitors. In particular, (S)-N-(2-oxo-3-oxetanyl)biphenyl-4-carboxamide (7h) was more potent than 7a at inhibiting recombinant rat NAAA activity (7a, IC50 = 420 nM; 7h, IC50 = 115 nM) in vitro and at reducing carrageenan-induced leukocyte infiltration in vivo.

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Enterobactin and Enantioenterobactin

Cited by 31 publications

References 21 publications

Macrocycles Derived from Cinchona Alkaloids: A Thermodynamic vs Kinetic Study

Macrocycles Derived from Cinchona Alkaloids: A Thermodynamic vs Kinetic Study

Catechol Siderophore Transport by Vibrio cholerae

Synthesis and Structure−Activity Relationships of N-(2-Oxo-3-oxetanyl)amides as N-Acylethanolamine-hydrolyzing Acid Amidase Inhibitors

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