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)

The compartimentation and the relative strength of binding of the enzymes lipoamide dehydrogenase (LIPDH), citrate synthase (CS), and beta-hydroxyacyl-coenzyme A-dehydrogenase (HADH) in mitochondria isolated from bovine muscle (M. sternomandibularis) were studied using the following methods: Availability of the enzymes for proteases before and after opening of the intracrystal line space and after disintegration of the mitochondrial membranes; release of the enzymes after different treatments of the mitochondria: homogenization with phosphate buffer plus Triton X-100; suspension in dest. water and saccharose-tris buffer with and without added digitonin; ultrasonic treatment; freezing and thawing. From the results it can be concluded that the three enzymes are bound to the inner surface of the inner membrane of the mitochondrion, and that the binding strength increases according to the series CS less than HADH less than LIPDH.
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PMID:[Lipoamide dehydrogenase, citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase of skeletal muscle. II. Compartmentalization of the enzymes in muscle mitochondria and their relative binding capacity]. 638 Jan 31

NADH:ubiquinone reductase (complex I) of the mitochondrial inner membrane respiratory chain binds a number of mitochondrial matrix NAD-linked dehydrogenases. These include pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, mitochondrial malate dehydrogenase, and beta-hydroxyacyl-CoA dehydrogenase. No binding was detected between complex I and cytosolic malate dehydrogenase, glutamate dehydrogenase, NAD-isocitrate dehydrogenase, lipoamide dehydrogenase, citrate synthase, or fumarase. The dehydrogenases that bound to complex I did not bind to a preparation of complex II and III, nor did they bind to liposomes. The binding of pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, and mitochondrial malate dehydrogenase to complex I is a saturable process. Based upon the amount of binding observed in these in vitro studies, there is enough inner membrane present in the mitochondria to bind the dehydrogenases in the matrix space. The possible metabolic significance of these interactions is discussed.
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PMID:Complex I binds several mitochondrial NAD-coupled dehydrogenases. 643 16

It is to be expected that changes in the subcellular distribution of the mitochondrial enzymes lipoamide dehydrogenase (LIPDH), citrate synthase (CS) and beta-hydroxyacyl-CoA-dehydrogenase (HADH) in the muscle tissue give information on the type and the extent of damage of mitochondria during storage and treatment of meats; such changes may be also used as basis of methods for the differentiation between fresh and frozen/thawed meat. Standard methods for the determination of the activities of LIPDH, CS, and HADH in tissue extract and muscle press juice are described. The influence of enzyme concentration, pH and temperature on the enzyme activities in muscle extract was investigated. Furthermore the error in the enzyme analyses by the standard methods was determined.
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PMID:[Lipoamide dehydrogenase, citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase in skeletal muscle. I. Determination of activity in tissue extracts]. 654 96

The extractable total activities of lipoamide dehydrogenase (LIPDH), citrate synthase (CS), and beta-hydroxyacyl-CoA-dehydrogenase (HADH) were determined in different muscles (longissimus dorsi, semimembranosus, diaphragma) from cattle and pigs, and in the breast and leg muscles from chicken and ducks. The subcellular distribution of these enzymes was elucidated by determination of the enzyme activities in the pressjuice of the intact muscle tissue. In the muscles of the different species positive correlations between myoglobin content and the activities of the three enzymes were found, which were closer for pigs and chicken than for cattle and ducks. At least 90 percent of the total activity of LIPDH, CS and HADH was located in the mitochondria.
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PMID:[Lipoamide dehydrogenase, citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase of skeletal muscle. III. Activity and subcellular distribution in light and dark musculature of cattle, swine and poultry]. 654 97

Postmortem storage of bovine and porcine semimembranosus muscle under refrigeration (+2 degrees C) for 14 days did not result in a significant decrease of the total activity of the mitochondrial enzymes citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase, but caused a loss of the activity of lipoamide dehydrogenase. During storage of the muscle tissue there was no detectable release of the three enzymes from the mitochondria into the sarcoplasmic fluid. Therefore, storage of muscle under the conditions used seems not to result in any remarkable damage of the inner membrane of the mitochondrion.
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PMID:[Lipoamide dehydrogenase, citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase in skeletal muscles. IV. The effect of storage of bovine and swine muscles at 2 degrees C on their activity and subcellular distribution]. 654 95

Postmortem storage under refrigeration (+2 degrees C) for 7 days of the semimembranosus muscles from sheep, hare and roe deer and of the breast and leg muscles from chicken and duck did not result in a significant decrease of the total activities of the mitochondrial enzymes citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase but caused a loss of the activity of lipoamide dehydrogenase (except in chicken muscle). During storage of the muscle tissue, there was no detectable release of the three enzymes from the mitochondria into the sarcoplasmic fluid except in venison at the point of spoilage. Therefore, storage of muscle under our conditions does not result in notable damage of the inner membrane of the mitochondrion.
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PMID:[Lipoamide dehydrogenase, citrate synthase and beta-hydroxyacyl-CoA-dehydrogenase of skeletal muscle. V. Effect of storage of muscles from sheep, game and poultry at +2 degrees C on activity and subcellular distribution]. 654 54

The activity of 22 enzymes of energy metabolism was determined in m. vastus lateralis quadricipitis of 14 adolescents aged 13-15 years (7 girls) and 14 adults aged 22 to 42 years (7 female subjects). The measurements were performed kinetically, at 37 degrees C, using optimal or near-to-optimal procedures. With the exception of one enzyme, enolase, no differences between sexes were observed in the two age groups. Glycolytic enzymes, including fructose-6-phosphate kinase, showed no significant differences in their activity in adults as compared to adolescents. The activity of enolase was lower in females of both age groups, but no difference due to age was found in this respect. Of the oxidative enzymes studied, only citrate synthase showed no significant difference in adults vs adolescents, whereas the activities of lipoamide dehydrogenase (+ 40%), NADP-isocitrate dehydrogenase (+ 44%), fumarase (+ 24.5%), total malate dehydrogenase (+ 42.2%) and NADH-dehydrogenase (+ 39%) were all significantly higher in the latter group. Aspartate aminotransferase was also 44% higher in adolescents. The possible physiological importance of these observations is discussed with regard to the functional capacity of the skeletal muscle. The hypothesis was considered that adolescents of this age may have a glycolytic capacity comparable to adults, but that they may oxidize pyruvate at a rate higher than adults.
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PMID:Enzyme activities in skeletal muscle of 13-15 years old adolescents. 705 78

FarR (formerly P30) has been identified as a fatty acid and fatty acyl-CoA responsive DNA-binding protein. It is encoded by the farR gene (g30) in the citric acid cycle gene cluster of E. coli (gltA-sdhCDAB-sucABCD-farR). The amplified FarR protein specifically bound to the farR promoter (PfarR) and exhibited weak binding to the citrate synthase and lipoamide dehydrogenase promoters. Binding at PfarR was abolished by long-chain fatty acids and their CoA thioesters. In DNaseI footprints, FarR binding at PfarR protected two sites, each characterised by two related 10-bp direct repeats. It is suggested that FarR autoregulates farR expression and may modulate citric acid cycle expression in response to long-chain fatty acids.
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PMID:Identification of a fatty acyl responsive regulator (FarR) in Escherichia coli. 780 34

Mitochondrial enzyme activities (cytochrome c-oxidase = COX, carnitine acyl-transferase = CAT, citrate synthase = CS, lipoamide dehydrogenase = lipDH from the pyruvate-dehydrogenase complex, lactate dehydrogenase = LDH, and malate-dehydrogenase = MDH) were measured from progressive myopathy/encephalomyopathy. Cytochrome oxidase (COX) deficiency was detected from muscle or liver tissues, adult type of COX defectus had been diagnosed in 1 case and infantile type in further 6 cases. The 3 familial atactic children showed decreased activity of carnitine acetyl-transferase, too.
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PMID:[Specific enzyme diagnosis in mitochondrial myopathies and encephalomyopathies]. 817 Jun 74

To assess the suitability of lymphocytes for patient diagnosis and carrier detection of lipoamide dehydrogenase deficiency, the activity of lipoamide dehydrogenase was determined in lymphocytes of six patients, seven obligate heterozygotes and 32 healthy controls. In healthy controls, lipoamide dehydrogenase activity was 80.7 +/- 23.6 nmol/min/mg protein, in obligate heterozygotes it was 36.0 +/- 12.1 nmol/min/mg protein and in the patients it was 13.3 +/- 5.1 nmol/min/mg protein. For the purpose of standardization, the results were also calculated as lipoamide dehydrogenase/citrate synthase activity ratio. The activity of lipoamide dehydrogenase and the lipoamide dehydrogenase/citrate synthase ratio differed significantly between the three groups (P < 0.005). We conclude that lymphocytes are suitable for the diagnosis of lipoamide dehydrogenase deficiency and for carrier detection.
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PMID:Lipoamide dehydrogenase activity in lymphocytes. 902 30


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