Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.2.1.13 (acetyl-CoA synthetase)
 451 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The incorporation of labelled glucose into lipid by liver slices from sheep and cows is considerably less than that by liver slices from the rat, although oxidation to carbon dioxide occurs to a similar extent. ATP citrate lyase and NADP malate dehydrogenase are inactive in both sheep and cow liver but active in rat liver. The absence of the citrate-cleavage pathway of lipogenesis in ruminant liver has been confirmed by the negligible amounts of C-3 of aspartate incorporated into fatty acids. 2. Considerable amounts of [(14)C]acetate are incorporated into fatty acids and non-saponifiable lipid in rat and ruminant liver. Acetyl-CoA synthetase, the initial enzyme in the metabolism of acetate, has a high activity in liver from rat and ruminants. 3. In adipose tissue from ruminants more acetate than glucose is converted into lipids, whereas the converse is true in rat adipose tissue. The greater incorporation of [(14)C]acetate into fatty acids in adipose tissue from the ruminant as compared with the non-ruminant may be caused, in part, by the higher activity of acetyl-CoA synthetase activity in the ruminant. 4. The results suggest that, in both liver and adipose tissue from ruminants, acetate is a more important source of lipid than glucose. 5. Two enzymes of the hexose monophosphate shunt, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, are active in both tissues and from the three species.
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PMID:The relative significance of acetate and glucose as precursors for lipid synthesis in liver and adipose tissue from ruminants. 558 95

Oxidative metabolism in the in vivo canine myocardium was studied noninvasively using 13C-enriched acetate and non-steady state 13C NMR techniques. Under low workload conditions, the myocardium oxidized the infused [2-13C]acetate and incorporated the labeled carbon into the glutamate pool as expected. This conclusion stems from the rapid enrichment of the C-2, C-3, and C-4 carbons of glutamic acid both under in vivo conditions and in extracts. Surprisingly, [2-13C]acetate uptake was not observed at high workloads as reflected by an absence of glutamate pool enrichment at these rate pressure products. Rather, the myocardium selected its substrate from an endogenous pool. Since free acetate can directly cross the inner mitochondrial membrane and be converted to acetyl-CoA through acetyl-CoA synthetase, these results support workload-dependent regulation of substrate access to the mitochondrial CoASH pool. As such, we advance the hypothesis that the selection of substrate for condensation with CoASH and subsequent oxidation in the tricarboxylic acid cycle is regulated kinetically through the Km values of the appropriate condensation enzymes and through the absolute levels of free CoASH in the mitochondria.
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PMID:Dynamic 13C NMR analysis of oxidative metabolism in the in vivo canine myocardium. 825 51