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1.
Molecules ; 26(21)2021 Nov 06.
Article in English | MEDLINE | ID: mdl-34771130

ABSTRACT

The genus Nothofagus is one of the most abundant in the subantarctic Patagonian forests. Five species inhabit these ecosystems, three evergreen (Nothofagus betuloides, Nothofagus dombeyi, and Nothofagus nitida) and two deciduous (Nothofagus pumilio and Nothofagus antarctica). This is the first report on the levels of secondary metabolites and the antioxidant capacity of Patagonian tree species growing in natural environments. The aim of this work was to carry out a phytochemical screening, to determine the antioxidant capacity, the sun protection factor, and the α-glucosidase and tyrosinase inhibitory activity of foliar extracts of the five previous species. Besides, Aristotelia chilensis and Berberis microphylla, two species of Patagonian shrubs growing in the same forests, were used as reference. N. dombeyi was the Nothofagus with the best antioxidant capacity. B. microphylla differed from all studied species. Moreover, the Nothofagus was split into two groups. N. betuloides and N. dombeyi are the most similar species to A. chilensis. The α-glucosidase was completely inhibited by all studied extracts. Furthermore, N. antarctica, N.pumilio, and N. nitida inhibited about 70% of the tyrosinase activity. All the results found in this study for the species of the genus Nothofagus support further research on their potential beneficial properties for human health.


Subject(s)
Antioxidants/pharmacology , Enzyme Inhibitors/pharmacology , Phytochemicals/pharmacology , Trees/chemistry , Antioxidants/chemistry , Antioxidants/metabolism , Benzothiazoles/antagonists & inhibitors , Biphenyl Compounds/antagonists & inhibitors , Chile , Drug Evaluation, Preclinical , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/metabolism , Forests , Humans , Monophenol Monooxygenase/antagonists & inhibitors , Monophenol Monooxygenase/metabolism , Phytochemicals/chemistry , Phytochemicals/metabolism , Picrates/antagonists & inhibitors , Species Specificity , Sulfonic Acids/antagonists & inhibitors , Trees/metabolism , alpha-Glucosidases/metabolism
2.
Int J Med Chem ; 2019: 2592609, 2019.
Article in English | MEDLINE | ID: mdl-31815016

ABSTRACT

Polyphenols are secondary metabolites of plants and include a variety of chemical structures, from simple molecules such as phenolic acids to condensed tannins and highly polymerized compounds. Caffeic acid (3,4-dihydroxycinnamic acid) is one of the hydroxycinnamate metabolites more widely distributed in plant tissues. It is present in many food sources, including coffee drinks, blueberries, apples, and cider, and also in several medications of popular use, mainly those based on propolis. Its derivatives are also known to possess anti-inflammatory, antioxidant, antitumor, and antibacterial activities, and can contribute to the prevention of atherosclerosis and other cardiovascular diseases. This review is an overview of the available information about the chemical synthesis and antioxidant activity of caffeic acid derivatives. Considering the relevance of these compounds in human health, many of them have been the focus of reviews, taking as a center their obtaining from the plants. There are few revisions that compile the chemical synthesis methods, in this way, we consider that this review does an important contribution.

3.
Biochem Biophys Res Commun ; 405(1): 134-9, 2011 Feb 04.
Article in English | MEDLINE | ID: mdl-21219871

ABSTRACT

Glutamyl-tRNA reductase (GluTR) is the first enzyme committed to tetrapyrrole biosynthesis by the C(5)-pathway. This enzyme transforms glutamyl-tRNA into glutamate-1-semi-aldehyde, which is then transformed into 5-amino levulinic acid by the glutamate-1-semi-aldehyde 2,1-aminomutase. Binding of heme to GluTR seems to be relevant to regulate the enzyme function. Recombinant GluTR from Acidithiobacillus ferrooxidans an acidophilic bacterium that participates in bioleaching of minerals was expressed in Escherichia coli and purified as a soluble protein containing type b heme. Upon control of the cellular content of heme in E. coli, GluTR with different levels of bound heme was obtained. An inverse correlation between the activity of the enzyme and the level of bound heme to GluTR suggested a control of the enzyme activity by heme. Heme bound preferentially to dimeric GluTR. An intact dimerization domain was essential for the enzyme to be fully active. We propose that the cellular levels of heme might regulate the activity of GluTR and ultimately its own biosynthesis.


Subject(s)
Acidithiobacillus/enzymology , Aldehyde Oxidoreductases/metabolism , Heme/metabolism , Acidithiobacillus/genetics , Aldehyde Oxidoreductases/chemistry , Aldehyde Oxidoreductases/genetics , Catalysis , Escherichia coli/genetics , Protein Multimerization , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism
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