The Coenzyme A Level Modulator Hopantenate (HoPan) Inhibits Phosphopantotenoylcysteine Synthetase Activity

2021 ◽  
Author(s):  
Konrad J. Mostert ◽  
Nandini Sharma ◽  
Marianne van der Zwaag ◽  
Roxine Staats ◽  
Lizbé Koekemoer ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Synthetase Activity

scholarly journals Capsaicin, nonivamide and trans-pellitorine decrease free fatty acid uptake without TRPV1 activation and increase acetyl-coenzyme A synthetase activity in Caco-2 cells

2015 ◽  
Vol 6 (1) ◽  
pp. 172-184 ◽  
Author(s):  
Barbara Rohm ◽  
Annett Riedel ◽  
Jakob P. Ley ◽  
Sabine Widder ◽  
Gerhard E. Krammer ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Coenzyme A ◽  
Fatty Acid Uptake ◽  
Synthetase Activity ◽  
Acid Uptake ◽  
Structural Element ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

The effects of capsaicin, nonivamide,trans-pellitorine and vanillin as the basic structural element of all vanilloids on the mechanisms of intestinal fatty acid uptake in differentiated intestinal Caco-2 cells were studied.

scholarly journals Identification of an Acetoacetyl Coenzyme A Synthetase-Dependent Pathway for Utilization of l-(+)-3-Hydroxybutyrate in Sinorhizobium meliloti

2002 ◽  
Vol 184 (6) ◽  
pp. 1571-1577 ◽  
Author(s):  
Punita Aneja ◽  
Renata Dziak ◽  
Guo-Qin Cai ◽  
Trevor C. Charles
Keyword(s):  
Sinorhizobium Meliloti ◽  
Direct Evidence ◽  
Coenzyme A ◽  
Sole Source ◽  
Degradation Pathway ◽  
Synthetase Activity ◽  
Gene Encoding ◽  
Carbon Store ◽  
Utilization Pathway ◽  
Dependent Pathway

ABSTRACT d-(−)-3-Hydroxybutyrate (DHB), the immediate depolymerization product of the intracellular carbon store poly-3-hydroxybutyrate (PHB), is oxidized by the enzyme 3-hydroxybutyrate dehydrogenase to acetoacetate (AA) in the PHB degradation pathway. Externally supplied DHB can serve as a sole source of carbon and energy to support the growth of Sinorhizobium meliloti. In contrast, wild-type S. meliloti is not able to utilize the l-(+) isomer of 3-hydroxybutyrate (LHB) as a sole source of carbon and energy. In this study, we show that overexpression of the S. meliloti acsA2 gene, encoding acetoacetyl coenzyme A (acetoacetyl-CoA) synthetase, confers LHB utilization ability, and this is accompanied by novel LHB-CoA synthetase activity. Kinetics studies with the purified AcsA2 protein confirmed its ability to utilize both AA and LHB as substrates and showed that the affinity of the enzyme for LHB was clearly lower than that for AA. These results thus provide direct evidence for the LHB-CoA synthetase activity of the AcsA2 protein and demonstrate that the LHB utilization pathway in S. meliloti is AcsA2 dependent.

scholarly journals The effects of high dietary supplements of copper sulphate on pantothenic acid metabolism in the chick

1981 ◽  
Vol 45 (2) ◽  
pp. 431-439 ◽  
Author(s):  
Eva A. Latymer ◽  
Marie E. Coates
Keyword(s):  
Fatty Acid ◽  
Dietary Supplements ◽  
Copper Sulphate ◽  
Acid Metabolism ◽  
Coenzyme A ◽  
Pantothenic Acid ◽  
Fatty Acid Synthetase ◽  
Synthetase Activity ◽  
Low Doses ◽  
Calcium Pantothenate

1. The effects of incorporation of copper sulphate supplying 250 mg copper/kg semi-purified diet with graded amounts of calcium pantothenate (CaPa) were studied in chicks.2. When the doses of CaPa were marginally adequate or less the Cu supplementation induced severe signs of pantothenic acid (PaA) deficiency.3. Livers of the Cu-treated birds given low doses of PaA had lower concentrations of total and bound PaA than those of the corresponding control birds. The bound:total PaA value was also reduced.4. The amount and concentration of coenzyme A (CoA) were significantly less in the livers of Cu-treated chicks. Fatty acid synthetase activity was not reduced.5. It is suggested that high dietary supplements of CuSO4, induce PaA deficiency through interference in the biosynthesis of CoA.

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