scholarly journals Inhibitory effects of garcinone E on fatty acid synthase

RSC Advances ◽  
2018 ◽  
Vol 8 (15) ◽  
pp. 8112-8117 ◽  
Author(s):  
Yan Liang ◽  
Di Luo ◽  
Xuan Gao ◽  
Hao Wu
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Time Dependent ◽  
Inhibitory Effects ◽  
Irreversible Inhibition

Garcinone E exhibits both fast-binding reversible and time-dependent irreversible inhibition on the activity of fatty acid synthase.

Inhibitory effects of sea buckthorn procyanidins on fatty acid synthase and MDA-MB-231 cells

Tumor Biology ◽  
2014 ◽  
Vol 35 (10) ◽  
pp. 9563-9569 ◽  
Author(s):  
Yi Wang ◽  
Fangyuan Nie ◽  
Jian Ouyang ◽  
Xiaoyan Wang ◽  
Xiaofeng Ma
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Sea Buckthorn ◽  
Inhibitory Effects

scholarly journals Inhibitory effects of thioethers on fatty acid synthase and 3T3-L1 cells

2009 ◽  
Vol 25 (2) ◽  
pp. 290-295 ◽  
Author(s):  
Xue-Bing Sun ◽  
Jiong Zhao ◽  
Xiao-Feng Ma ◽  
Wei-Xi Tian
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Inhibitory Effects

scholarly journals Aster glehni F. Schmidt Extract Modulates the Activities of HMG-CoA Reductase and Fatty Acid Synthase

Plants ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2287
Author(s):  
Hyunbeom Lee ◽  
Hyoung Ja Kim ◽  
Hyungi Chae ◽  
Na Eun Yoon ◽  
Byung Hwa Jung
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Therapeutic Potential ◽  
Methyl Esters ◽  
Acid Synthesis ◽  
Inhibitory Effect ◽  
Lipid Lowering ◽  
Inhibitory Effects ◽  
Hmg Coa Reductase ◽  
Coa Reductase

Aster glehni F. Schmidt (AG), is a natural product known to have anti-obesity effects, but the mechanism underlying these effects is not well documented. We hypothesized that AG may have inhibitory effects on enzymes related to lipid accumulation. Herein, AG fractions were tested against HMG-CoA reductase (HMGR) and fatty acid synthase (FAS), two important enzymes involved in cholesterol and fatty acid synthesis, respectively. We found that dicaffeoylquinic acid (DCQA) methyl esters present in AG are largely responsible for the inhibition of HMGR and FAS. Since free DCQA is a major form present in AG, we demonstrated that a simple methylation of the AG extract could increase the overall inhibitory effects against those enzymes. Through this simple process, we were able to increase the inhibitory effect by 150%. We believe that our processed AG effectively modulates the HMGR and FAS activities, providing promising therapeutic potential for cholesterol- and lipid-lowering effects.

scholarly journals Inhibitory Effects of Allium Vegetable Extracts on Fatty Acid Synthase

2009 ◽  
Vol 15 (3) ◽  
pp. 343-346 ◽  
Author(s):  
Xue-Bing SUN ◽  
Wei-Xi TIAN
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Inhibitory Effects

scholarly journals Irreversible inhibition of fatty acid synthase from rat mammary gland with S-(4-bromo-2,3-dioxobutyl)-CoA. Effect on the partial reactions, protection by substrates and stoichiometry studies

1982 ◽  
Vol 207 (2) ◽  
pp. 291-296 ◽  
Author(s):  
P R Clements ◽  
R E Barden ◽  
P M Ahmad ◽  
M B Chisner ◽  
F Ahmad
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Bimolecular Reaction ◽  
Alkylation Reaction ◽  
Thiol Groups ◽  
Partial Reaction ◽  
Nitrobenzoic Acid ◽  
Irreversible Inhibition ◽  
Rat Mammary Gland

Fatty acid synthase from lactating rat mammary gland is rapidly and irreversibly inhibited by S-(4-bromo-2,3-dioxobutyl)-CoA. Of the seven partial reactions catalysed by the enzyme, the inhibition of the overall catalytic activity is closely paralleled only by inhibition of the beta-oxoacyl synthase (condensing) partial reaction. Three partial reactions. Beta-oxoacyl reductase, beta-hydroxyacyl dehydratase and enoyl reductase, are inhibited to a modest degree. The three partial reactions known to involve an acyl-CoA/CoA-binding site, acetyl acyltransferase, malonyl acyltransferase and palmitoyl thioesterase, are not inhibited by S-(4-bromo-2,3-dioxobutyl)-CoA. The modification process does not cause the enzyme to dissociate into catalytically incompetent monomers. Stoichiometric studies suggest that approx. 6 mol of reagent are incorporated per mol of totally inhibited enzyme (dimer). The formation of acylated enzyme from either acetyl-CoA or malonyl-CoA protects the enzyme equally well against S-(4-bromo-2,3-dioxobutyl)-CoA. Also, pretreatment of the enzyme with 5,5′-dithiobis-(2-nitrobenzoic acid), a thiol-specific reagent reported to block essential thiol groups in the condensing partial reaction, protects against inhibition by the reagent. On the other hand, the presence of up to 770 microM-S-acetonyl-CoA or dethio-CoA does not protect the enzyme from irreversible inhibition. Together, the results suggest that the primary inhibitory process is a bimolecular reaction resulting in alkylation of essential thiol groups in the condensing partial reaction: this process does not require the obligatory formation of a Michaelis-Menten complex of enzyme and reagent before the alkylation reaction.

scholarly journals Inhibitory Effects of 4-(4-Methylbenzamino)benzoate on Adipocyte Differentiation

2015 ◽  
Vol 2015 ◽  
pp. 1-4
Author(s):  
Jin Taek Hwang ◽  
Sanghee Kim ◽  
Bo-ra Yoon ◽  
Inwook Choi ◽  
Sang Yoon Choi
Keyword(s):  
Fatty Acid ◽  
Glucose Metabolism ◽  
Fatty Acid Synthase ◽  
Adipocyte Differentiation ◽  
Ppar Gamma ◽  
Gamma Activity ◽  
Dependent Manner ◽  
Inhibitory Effects ◽  
Concentration Dependent Manner ◽  
Cellular Expression

The potent suppression of adipocyte differentiation by 4-(4-methylbenzamino)benzoate was discovered during the search for new antiobesity compounds. 4-(4-methylbenzamino)benzoate was observed to suppress adipocyte differentiation in 3T3-L1 cells by 96.8% at 50 μM without cytotoxicity. In addition, 4-(4-methylbenzamino)benzoate reduced the cellular expression of fatty acid synthase in a concentration-dependent manner, as well as suppressing PPAR-gamma activity, which controls fatty acid storage and glucose metabolism. Based on these results, 4-(4-methylbenzamino)benzoate shows potential as an antiobesity material.

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