نتایج جستجو برای: long chain acyl coa synthetase

تعداد نتایج: 1084410  

Objective(s): This study intended to investigate the effects of Ginsenoside-Rbl (Gs-Rbl) on fatty acid β-oxidation (FAO) in rat failing heart and to identify potential mechanisms of Gs-Rbl improving heart failure (HF) by FAO pathway dependent on AMP-activated protein kinase (AMPK). Materials and Methods: Rats with chronic HF, induced by adriamycin (Adr), were randomly grouped into 7 groups. Gs-...

Journal: :The Journal of biological chemistry 2001
N J Faergeman P N Black X D Zhao J Knudsen C C DiRusso

Exogenous long-chain fatty acids are activated to coenzyme A derivatives prior to metabolic utilization. In the yeast Saccharomyces cerevisiae, the activation of these compounds prior to metabolic utilization proceeds through the fatty acyl-CoA synthetases Faa1p and Faa4p. Faa1p or Faa4p are essential for long-chain fatty acid import, suggesting that one or both of these enzymes are components ...

Journal: :Journal of lipid research 2004
Douglas G Mashek Karin E Bornfeldt Rosalind A Coleman Johannes Berger David A Bernlohr Paul Black Concetta C DiRusso Steven A Farber Wen Guo Naohiro Hashimoto Varsha Khodiyar Frans A Kuypers Lois J Maltais Daniel W Nebert Alessandra Renieri Jean E Schaffer Andreas Stahl Paul A Watkins Vasilis Vasiliou Tokuo T Yamamoto

By consensus, the acyl-CoA synthetase (ACS) community, with the advice of the human and mouse genome nomenclature committees, has revised the nomenclature for the mammalian long-chain acyl-CoA synthetases. ACS is the family root name, and the human and mouse genes for the long-chain ACSs are termed ACSL1,3-6 and Acsl1,3-6, respectively. Splice variants of ACSL3, -4, -5, and -6 are cataloged. Su...

2013
Christoph Wiesinger Markus Kunze Günther Regelsberger Sonja Forss-Petter Johannes Berger

Background: ABCD1 is a peroxisomal ABC transporter whose dysfunction causes X-linked adrenoleukodystrophy (X-ALD). Results: β-Oxidation of C26:0 as well as C22:0 acyl-CoA esters is impaired in X-ALD. ABCD3 accounts for residual β-oxidation activity in XALD fibroblasts. Conclusion: ABCD1 mediates very long-chain acyl-CoA ester β-oxidation without need for additional re-esterification by an acyl-...

Journal: :Plant physiology 1981
J Joyard P K Stumpf

The chloroplast envelope is the site of a very active long-chain acylcoenzyme A (CoA) synthetase. Furthermore, we have recently shown that an acyl CoA thioesterase is also associated with envelope membrane (Joyard J, PK Stumpf 1980 Plant Physiol 65: 1039-1043). To clarify the interacting roles of both the acyl-CoA thioesterase and the acyl-CoA synthetase, the formation of acyl-CoA in envelope m...

Journal: :Journal of lipid research 1996
P A Watkins A E Howard S J Gould J Avigan S J Mihalik

In Refsum disease, disorders of peroxisome biogenesis, and rhizomelic chondrodysplasia punctata, pathological accumulation of phytanic acid results from impaired alpha-oxidation of this branched-chain fatty acid. Previous studies from this laboratory indicated that activation of phytanic acid to its CoA derivative precedes its alpha-oxidation in peroxisomes. It was reported that this reaction i...

Journal: :The Journal of biological chemistry 1979
G F Tutwiler P Dellevigne

Using isolated hepatocytes from fasted rats, the oral hypoglycemic agents, Z-tetradecylglycidic acid (McN3802) and its methyl ester (McN-3716) inhibited (concentrations down to 5 x lo-’ M) the oxidation of palmitate to CO2 and ketones but not the oxidation of octauoate or palmitoylcarnitine. The antiketogenic effect which occurs at concentrations as low as lo-’ M was accompanied by a lowered P-...

Journal: :The Biochemical journal 1991
A M Bakken M Farstad H Holmsen

Apparent Km values have been determined for the substrates ATP, CoA and fatty acids for the long-chain acyl-CoA synthetase (EC 6.2.1.3) reaction in lysates of human blood platelets. The apparent Km for ATP was higher for saturated fatty acids (C12:0 to C18:0) than for unsaturated acids (C18:1 to C22:6). Other apparent Km values were very similar for all long-chain fatty acids tested. Palmitic a...

Journal: :The Biochemical journal 1997
N J Faergeman J Knudsen

The intracellular concentration of free unbound acyl-CoA esters is tightly controlled by feedback inhibition of the acyl-CoA synthetase and is buffered by specific acyl-CoA binding proteins. Excessive increases in the concentration are expected to be prevented by conversion into acylcarnitines or by hydrolysis by acyl-CoA hydrolases. Under normal physiological conditions the free cytosolic conc...

Journal: :The Journal of biological chemistry 1990
C B Hesler C Olymbios D Haldar

Transverse-plane topography of mitochondrial outer-membrane long-chain acyl-CoA synthetase was investigated using proteases as probes for exposure of crucial domains, i.e. domains containing the active site or otherwise required for enzymatic activity. Incubation of intact mitochondria with the nonspecific proteases proteinase K and subtilisin resulted in a time-dependent loss of 90% or more of...

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