scholarly journals Tuneable radical cyclisations: a tin-free approach towards tricyclic and spirocyclic heterocycles via a common precursor

RSC Advances ◽  
2014 ◽  
Vol 4 (36) ◽  
pp. 18930-18932 ◽  
Author(s):  
B. Patel ◽  
G. Saviolaki ◽  
C. Ayats ◽  
M. A. E. Garcia ◽  
T. Kapadia ◽  
...  

A novel common precursor approach towards both tricyclic and spirocyclic heterocycles is described. Cyclisations are based on thiyl radical/isocyanide methodology and avoid the use of tin.

2018 ◽  
Author(s):  
Andrea Pérez-Villa ◽  
Thomas Georgelin ◽  
Jean-François Lambert ◽  
Marie-Christine Maurel ◽  
François Guyot ◽  
...  

Understanding the mechanism of spontaneous formation of ribonucleotides under realistic prebiotic conditions is a key open issue of origins-of-life research. In cells, <i>de novo</i> and salvage nucleotide enzymatic synthesis combines 5-phospho-α -D-ribose-1-diphosphate ( α-PRPP) and nucleobases. Interestingly, these reactants are also known as prebiotically plausible compounds. Combining ab initio simulations with mass spectrometry experiments, we compellingly demonstrate that nucleobases and α -PRPP spontaneously combine, through the same facile mechanism, forming both purine and pyrimidine ribonucleotides, under mild hydrothermal conditions. Surprisingly, this mechanism is very similar to the biological one, and yields ribonucleotides with the same anomeric carbon chirality as in biological systems. These results suggest that natural selection might have optimized – through enzymes – a pre-existing ribonucleotide formation mechanism, carrying it forward to modern life forms.


2017 ◽  
Author(s):  
Andrea Pérez-Villa ◽  
Thomas Georgelin ◽  
Jean-François Lambert ◽  
Marie-Christine Maurel ◽  
François Guyot ◽  
...  

Understanding the mechanism of spontaneous formation of ribonucleotides under realistic prebiotic conditions is a key open issue of origins-of-life research. In cells, <i>de novo</i> and salvage nucleotide enzymatic synthesis combines 5-phospho-α -D-ribose-1-diphosphate ( α-PRPP) and nucleobases. Interestingly, these reactants are also known as prebiotically plausible compounds. Combining ab initio simulations with mass spectrometry experiments, we compellingly demonstrate that nucleobases and α -PRPP spontaneously combine, through the same facile mechanism, forming both purine and pyrimidine ribonucleotides, under mild hydrothermal conditions. Surprisingly, this mechanism is very similar to the biological one, and yields ribonucleotides with the same anomeric carbon chirality as in biological systems. These results suggest that natural selection might have optimized – through enzymes – a pre-existing ribonucleotide formation mechanism, carrying it forward to modern life forms.


1993 ◽  
Vol 268 (6) ◽  
pp. 4300-4303
Author(s):  
P.M. Weers ◽  
W.J. Van Marrewijk ◽  
A.M. Beenakkers ◽  
D.J. Van der Horst
Keyword(s):  

1992 ◽  
Vol 267 (9) ◽  
pp. 6171-6177 ◽  
Author(s):  
M.J. Ligtenberg ◽  
L Kruijshaar ◽  
F Buijs ◽  
M van Meijer ◽  
S.V. Litvinov ◽  
...  
Keyword(s):  

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 705
Author(s):  
Awdhesh Kumar Mishra ◽  
Kwang-Hyun Baek

Salicylic acid (SA) is an active secondary metabolite that occurs in bacteria, fungi, and plants. SA and its derivatives (collectively called salicylates) are synthesized from chorismate (derived from shikimate pathway). SA is considered an important phytohormone that regulates various aspects of plant growth, environmental stress, and defense responses against pathogens. Besides plants, a large number of bacterial species, such as Pseudomonas, Bacillus, Azospirillum, Salmonella, Achromobacter, Vibrio, Yersinia, and Mycobacteria, have been reported to synthesize salicylates through the NRPS/PKS biosynthetic gene clusters. This bacterial salicylate production is often linked to the biosynthesis of small ferric-ion-chelating molecules, salicyl-derived siderophores (known as catecholate) under iron-limited conditions. Although bacteria possess entirely different biosynthetic pathways from plants, they share one common biosynthetic enzyme, isochorismate synthase, which converts chorismate to isochorismate, a common precursor for synthesizing SA. Additionally, SA in plants and bacteria can undergo several modifications to carry out their specific functions. In this review, we will systematically focus on the plant and bacterial salicylate biosynthesis and its metabolism.


FEBS Letters ◽  
1986 ◽  
Vol 208 (1) ◽  
pp. 67-72 ◽  
Author(s):  
A.J. Harmar ◽  
A. Armstrong ◽  
J.C. Pascall ◽  
K. Chapman ◽  
R. Rosie ◽  
...  

2016 ◽  
Vol 128 (28) ◽  
pp. 8213-8217 ◽  
Author(s):  
Takuya Hashimoto ◽  
Kohei Takino ◽  
Kazuki Hato ◽  
Keiji Maruoka
Keyword(s):  

1992 ◽  
Vol 58 (1) ◽  
pp. 119-125 ◽  
Author(s):  
Tsutomu Morikawa ◽  
Jun Uchida ◽  
Katsuhiko Imoto ◽  
Takeo Taguchi
Keyword(s):  

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