scholarly journals Triterpenoids Biosynthesis Regulation for Leaf Coloring of Wheel Wingnut (Cyclocaryapaliurus)

Forests ◽  
2021 ◽  
Vol 12 (12) ◽  
pp. 1733
Author(s):  
Caowen Sun ◽  
Shengzuo Fang ◽  
Xulan Shang
Keyword(s):  
Leaf Development ◽  
Mevalonic Acid ◽  
Metabolome Analysis ◽  
Accumulation Pattern ◽  
Treatment Of Diabetes ◽  
Acid Pathway ◽  
Coa Reductase ◽  
Hydroxymethylglutaryl Coa Reductase ◽  
Positive Results ◽  
Biosynthesis Regulation

Cyclocaryapaliurus leaves are rich in triterpenoids with positive results in the treatment of diabetes, antioxidation, and scavenging free radicals. C. paliurus red leaves have been found to contain higher flavonoids including anthocyanin, however, the triterpenoids accumulation pattern is still unclear. For the purpose of researching the triterpenoid accumulating mechanism during red new leaf development, transcriptome and metabolome analysis was conducted during C. paliurus the red leaf development process. The results uncovered that most triterpenoid ingredients were found to accumulate during leaves turning green, while the unique ingredients content including cyclocaric acid A, cyclocarioside I, cyclocarioside Ⅱand cyclocarioside Ⅲ decreased or remained unchanged. Functional structure genes (hydroxymethylglutaryl-CoA synthase, hydroxymethylglutaryl-CoA reductase, and farnesyl-diphosphate synthase) were identified for promoting triterpenoids accumulation mainly in the mevalonic acid pathway (MVA). Moreover, glycosyltransferase (UGT73C, UGT85A, and UGT85K) was also found attributed to triterpenoids accumulation. These findings provide information for a better understanding of the triterpenoid biosynthesis mechanism during leaf development and will be useful for targeted breeding.

scholarly journals Inhibition of Orbivirus Replication by Fluvastatin and Identification of the Key Elements of the Mevalonate Pathway Involved

Viruses ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1437
Author(s):  
Fauziah Mohd Jaafar ◽  
Baptiste Monsion ◽  
Mourad Belhouchet ◽  
Peter P. C. Mertens ◽  
Houssam Attoui
Keyword(s):  
Mevalonate Pathway ◽  
African Swine Fever Virus ◽  
Plaque Assay ◽  
African Swine Fever ◽  
Mevalonic Acid ◽  
Antiviral Effect ◽  
Structural Protein ◽  
Mevalonic Acid Pathway ◽  
Acid Pathway ◽  
Coa Reductase

Statin derivatives can inhibit the replication of a range of viruses, including hepatitis C virus (HCV, Hepacivirus), dengue virus (Flavivirus), African swine fever virus (Asfarviridae) and poliovirus (Picornaviridae). We assess the antiviral effect of fluvastatin in cells infected with orbiviruses (bluetongue virus (BTV) and Great Island virus (GIV)). The synthesis of orbivirus outer-capsid protein VP2 (detected by confocal immunofluorescence imaging) was used to assess levels of virus replication, showing a reduction in fluvastatin-treated cells. A reduction in virus titres of ~1.7 log (98%) in fluvastatin-treated cells was detected by a plaque assay. We have previously identified a fourth non-structural protein (NS4) of BTV and GIV, showing that it interacts with lipid droplets in infected cells. Fluvastatin, which inhibits 3-hydroxy 3-methyl glutaryl CoA reductase in the mevalonic acid pathway, disrupts these NS4 interactions. These findings highlight the role of the lipid pathways in orbivirus replication and suggest a greater role for the membrane-enveloped orbivirus particles than previously recognised. Chemical intermediates of the mevalonic acid pathway were used to assess their potential to rescue orbivirus replication. Pre-treatment of IFNAR(−/−) mice with fluvastatin promoted their survival upon challenge with live BTV, although only limited protection was observed.

scholarly journals The effects of statins on the mevalonic acid pathway in recombinant yeast strains expressing human HMG-CoA reductase

2013 ◽  
Vol 13 (1) ◽  
pp. 68 ◽  
Author(s):  
Agata Maciejak ◽  
Agata Leszczynska ◽  
Ilona Warchol ◽  
Monika Gora ◽  
Joanna Kaminska ◽  
...  
Keyword(s):  
Mevalonic Acid ◽  
Recombinant Yeast ◽  
Hmg Coa Reductase ◽  
Yeast Strains ◽  
Mevalonic Acid Pathway ◽  
Acid Pathway ◽  
Coa Reductase ◽  
Recombinant Yeast Strains

The Natural Products as Hydroxymethylglutaryl-Coa Reductase Inhibitors

2019 ◽  
Vol 16 (10) ◽  
pp. 1130-1137
Author(s):  
Hayrettin Ozan Gulcan ◽  
Serkan Yigitkan ◽  
Ilkay Erdogan Orhan
Keyword(s):  
Natural Products ◽  
Cardiovascular System ◽  
High Cholesterol ◽  
Chemical Structures ◽  
Reductase Inhibitors ◽  
Key Enzyme ◽  
Serious Disease ◽  
Coa Reductase ◽  
Hydroxymethylglutaryl Coa Reductase ◽  
Alternative Drugs

High cholesterol and triglyceride levels are mainly related to further generation of lifethreating metabolism disorders including cardiovascular system diseases. Therefore, hypercholesterolemia (i.e., also referred to as hyperlipoproteinemia) is a serious disease state, which must be controlled. Currently, the treatment of hypercholesterolemia is mainly achieved through the employment of statins in the clinic, although there are alternative drugs (e.g., ezetimibe, cholestyramine). In fact, the original statins are natural products directly obtained from fungi-like molds and mushrooms and they are potent inhibitors of hydroxymethylglutaryl-CoA reductase, the key enzyme in the biosynthesis of cholesterol. This review focuses on the first identification of natural statins, their synthetic and semi-synthetic analogues, and the validation of hydroxymethylglutaryl-CoA reductase as a target in the treatment of hypercholesterolemia. Furthermore, other natural products that have been shown to possess the potential to inhibit hydroxymethylglutaryl-CoA reductase are also reviewed with respect to their chemical structures.

scholarly journals Microbial biotransformation as a tool for drug development based on natural products from mevalonic acid pathway: A review

2015 ◽  
Vol 6 (1) ◽  
pp. 17-33 ◽  
Author(s):  
Mohamed-Elamir F. Hegazy ◽  
Tarik A. Mohamed ◽  
Abdelsamed I. ElShamy ◽  
Abou-El-Hamd H. Mohamed ◽  
Usama A. Mahalel ◽  
...  
Keyword(s):  
Natural Products ◽  
Drug Development ◽  
Mevalonic Acid ◽  
Mevalonic Acid Pathway ◽  
Acid Pathway

scholarly journals A hydroxymethylglutaryl-CoA reductase inhibitor synthesized by yeasts

1995 ◽  
Vol 132 (1-2) ◽  
pp. 39-43 ◽  
Author(s):  
Nina Gunde-Cimerman ◽  
Ana PlemenitaÅ¡ ◽  
Aleksa Cimerman
Keyword(s):  
Reductase Inhibitor ◽  
Coa Reductase ◽  
Hydroxymethylglutaryl Coa Reductase

scholarly journals 3-Hydroxy-3-methylglutaryl-coenzyme A reductase. A comparison of the modulation in vitro by phosphorylation and dephosphorylation to modulation of enzyme activity by feeding cholesterol- or cholestyramine-supplemented diets

1980 ◽  
Vol 185 (2) ◽  
pp. 435-441 ◽  
Author(s):  
Konstantinos A. Mitropoulos ◽  
Brian L. Knight ◽  
Bernard E. A. Reeves
Keyword(s):  
Microsomal Fraction ◽  
Coenzyme A ◽  
Maximal Activity ◽  
Kinetic Properties ◽  
Standard Diet ◽  
Microsomal Preparation ◽  
Phosphoprotein Phosphatase ◽  
Coa Reductase ◽  
Hydroxymethylglutaryl Coa Reductase ◽  
Coenzyme A Reductase

The activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (hydroxymethylglutaryl-CoA reductase) was considerably inhibited during incubation with ATP+Mg2+. The inactivated enzyme was reactivated on further incubation with partially purified cytosolic phosphoprotein phosphatase. The inactivation was associated with a decrease in the apparent Km of the reductase for hydroxymethylglutaryl-CoA, and this was reversed on reactivation. The slight increase in activity observed during incubation of microsomal fraction without ATP was not associated with a change in apparent Km and, unlike the effect of the phosphatase, was not inhibited by NaF. Liver microsomal fraction from rats given cholesterol exhibited a low activity of hydroxymethylglutaryl-CoA reductase with a low apparent Km for hydroxymethylglutaryl-CoA. Mícrosomal fraction from rats fed cholestyramine exhibited a high activity with a high Km. To discover whether these changes had resulted from phosphorylation and dephosphorylation of the reductase, microsomal fraction from rats fed the supplemented diets and the standard diet were inactivated with ATP and reactivated with phosphoprotein phosphatase. Inactivation reduced the maximal activity of the reductase in each microsomal preparation and also reduced the apparent Km for hydroxymethylglutaryl-CoA. There was no difference between the preparations in the degree of inactivation produced by ATP. Treatment with phosphatase restored both the maximal activity and the apparent Km of each preparation, but never significantly increased the activity above that observed with untreated microsomal fraction. It is concluded that hydroxymethylglutaryl-CoA reductase in microsomal fraction prepared by standard procedures is almost entirely in the dephosphorylated form, and that the difference in kinetic properties in untreated microsomal fraction from rats fed the three diets cannot be explained by differences in the degree of phosphorylation of the enzyme.

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