Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Substrate preferences of isolated mitochondria and maximal enzyme activities were used to assess the oxidative capacities of red muscle (RM) and white muscle (WM) of carp (Cyprinus carpio). A 14-fold higher activity of citrate synthase (CS) in RM reflects the higher mitochondrial density in this tissue. RM mitochondria oxidize pyruvate and fatty acyl carnitines (8:O, 12:O, 16:O) at similarly high rates. WM mitochondria oxidize these fatty acyl carnitines at 35-70% the rate of pyruvate, depending on chain length. WM has only half the carnitine palmitoyl transferase/CS ratio of RM, but similar ratios of beta-hydroxyacyl CoA dehydrogenase/CS. Ketone bodies are poor substrates for mitochondria from both tissues. In both tissues mitochondrial alpha-glycerophosphate oxidation was minimal, and alpha-glycerophosphate dehydrogenase was present at low activities, suggesting the alpha-glycerophosphate shuttle is of minor significance in maintaining cytosolic redox balance in either tissue. The mitochondrial oxidation rates of other substrates relative to pyruvate are as follows: alpha-ketoglutarate 90% (RM and WM); glutamate 45% (WM) and 70% (RM); proline 20% (WM) and 45% (RM). Oxidation of neutral amino acids (serine, glycine, alanine, beta-alanine) was not consistently detectable. These data suggest that RM and WM differ in mitochondrial properties as well as mitochondrial abundance. Whereas RM mitochondria appear to be able to utilize a wide range of metabolic fuels (fatty acids, pyruvate, amino acids but not ketone bodies), WM mitochondria appear to be specialized to use pyruvate.
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PMID:Oxidative properties of carp red and white muscle. 273 62

Ageing is associated with a reduction in muscle carnosine (beta-alanyl-L-histidine), but there are no data on the changes specifically in type I and type II muscle fibres. Given the higher carnosine content of type II fibers, changes observed in whole muscle may be secondary to a shift in fibre composition. Carnosine, beta-alanine, histidine, taurine, and citrate synthase (CS) and glycogen phosphorylase (Phos), were measured in pools of single muscle fibres from freeze-dried muscle biopsies of vastus lateralis of nine elderly sedentary subjects (65-80 years) with osteoarthritis of the knee and undergoing total knee replacement, and nine young moderately active healthy subjects (20-35 years). Fibres were characterised as type I or II by myosin ATPase activity. Carnosine was 53.2% lower in type II fibres of older subjects resulting in an estimated 7% (and most probably still higher) decline in intracellular physico-chemical buffering capacity. Younger subjects showed higher CS activities in type I and higher Phos activities in type II fibres. These differences were less apparent in elderly subjects. Possible causes for the change in the carnosine content are reduced physical activity, reduced meat intake, or the result of progressive denervation.
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PMID:Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects. 1696 7