Insights into the role of methionine synthase in the universal 13 C depletion in O - and N -methyl groups of natural products

2017 ◽  
Vol 635 ◽  
pp. 60-65 ◽  
Author(s):  
Katarzyna M. Romek ◽  
Agnieszka Krzemińska ◽  
Gérald S. Remaud ◽  
Maxime Julien ◽  
Piotr Paneth ◽  
...  
2014 ◽  
Vol 12 (2) ◽  
pp. 278-285 ◽  
Author(s):  
Pablo Urena-Torres ◽  
Jean Souberbielle
Keyword(s):  

Chemistry ◽  
2021 ◽  
Vol 3 (3) ◽  
pp. 821-830
Author(s):  
Davide De Simeis ◽  
Stefano Serra ◽  
Alessandro Di Fonzo ◽  
Francesco Secundo

Natural flavor and fragrance market size is expected to grow steadily due to the rising consumer demand of natural ingredients. This market request is guided by the general opinion that the production of natural compounds leads to a reduction of pollution, with inherent advantages for the environment and people’s health. The biotransformation reactions have gained high relevance in the production of natural products. In this context, few pieces of research have described the role of microalgae in the oxidation of terpenoids. In this present study, we questioned the role of microalgal based oxidation in the synthesis of high-value flavors and fragrances. This study investigated the role of three different microalgae strains, Chlorella sp. (211.8b and 211.8p) and Chlorococcum sp. (JB3), in the oxidation of different terpenoid substrates: α-ionone, β-ionone, theaspirane and valencene. Unfortunately, the experimental data showed that the microalgal strains used are not responsible for the substrate oxidation. In fact, our experiments demonstrate that the transformation of the four starting compounds is a photochemical reaction that involves the oxygen as oxidant. Even though these findings cast a shadow on the use of these microorganisms for an industrial purpose, they open a new possible strategy to easily obtain nootkatone in a natural way by just using an aqueous medium, oxygen and light.


Author(s):  
Songtao Dong ◽  
Xiangnan Guo ◽  
Fei Han ◽  
Zhonggui He ◽  
Yongjun Wang

2021 ◽  
Vol 10 (11) ◽  
pp. 2306
Author(s):  
Giuseppe Carota ◽  
Simone Ronsisvalle ◽  
Federica Panarello ◽  
Daniele Tibullo ◽  
Anna Nicolosi ◽  
...  

Although the epidemic caused by SARS-CoV-2 callings for international attention to develop new effective therapeutics, no specific protocol is yet available, leaving patients to rely on general and supportive therapies. A range of respiratory diseases, including pulmonary fibrosis, have been associated with higher iron levels that may promote the course of viral infection. Recent studies have demonstrated that some natural components could act as the first barrier against viral injury by affecting iron metabolism. Moreover, a few recent studies have proposed the combination of protease inhibitors for therapeutic use against SARS-CoV-2 infection, highlighting the role of viral protease in virus infectivity. In this regard, this review focuses on the analysis, through literature and docking studies, of a number of natural products able to counteract SARS-CoV-2 infection, acting both as iron chelators and protease inhibitors.


2018 ◽  
Vol 74 (1) ◽  
pp. 41-51
Author(s):  
Kazuhiro Yamada ◽  
Markos Koutmos

Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin-dependent methionine synthase (MS). MS is a large modular protein that utilizes an SN2-type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate-dependent methyltransferases, and MS in particular, function. Here, the structure of the folate-binding (Fol) domain of MS fromThermus thermophilusis reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate-binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C-terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM-barrel β8α8fold found in all other folate-binding domains, MS Fol domains exhibit a unique β8α7fold. It is posited that these structural differences are important for MS function.


2017 ◽  
Vol 94 ◽  
pp. 1145-1166 ◽  
Author(s):  
Zheng Wei Wong ◽  
Punniyakoti Veeraveedu Thanikachalam ◽  
Srinivasan Ramamurthy

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