Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Time-courses of changes in the activities of liver and kidney glucose-6-phosphatase [EC 3.1.3.9] and hepatic tryptophan pyrrolase [EC 1.13.1.12; TPO] in rats pre-fed high-protein diets for 5 days and then shifted to zero-protein diets were studied. Liver glucose-6-phosphatase activity decreased 1 day after the dietary shift but then increased and remained significantly higher than the 0 day value for the next 2 days. Changes in liver glycogen were found to be intimately and inversely related to liver glucose-6-phosphatase activity. Changes in kidney glucose-6-phosphatase activity paralleled the pattern of changes observed in liver activity. An initial decrease in TPO activity was followed by increased enzyme activity up to the 3rd day of the dietary shift. Later there was a rapid fall in tryptophan pyrrolase activity. Changes observed in these specific enzyme proteins differed from those observed in total tissue proteins. Alterations in the activities of these enzymes and changes in other parameters are compared with those observed earlier with the reverse type of dietary shift.
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PMID:Time-course of changes of liver tryptophan pyrrolase (tryptophan oxygenase) and liver and kidney glucose-6-phosphatase in rats shifted from high- to zero-protein diets. 625 15

Cathepsin D (EC 3.4.23.5), the insulin and glucagon degrading proteinase (IGP, EC 3.4.22.-) and the thiol-protein disulfide oxidoreductase (TPO, EC 1.8.4.2, 5.3.4.1) participate in the intracellular protein degradation, the last one also in post-protein-synthetic processing. The distribution of these enzymes was determined in isolated liver parenchymal cells, Kupffer cells and endothelial cells by means of immunochemical methods in order to further characterize these cell types. The cathepsin D content, expressed as microgram enzyme per mg protein, is about 3 fold higher in endothelial cells and about 5 to 24 fold higher in Kupffer cells than in parenchymal cells. This result confirms an earlier report which is based on the activity determination. The TPO concentration is highest in parenchymal cells with half of that concentration in Kupffer cells and one third in endothelial cells. About 0.5% of the total liver protein is represented by this enzyme. The IGP has been found to be totally absent in non-parenchymal cells. It represents, therefore, together with the glucose-6-phosphatase a valuable marker enzyme for parenchymal cells of rat liver.
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PMID:Distribution of thiol-protein disulfide oxidoreductase, insulin-glucagon proteinase and cathepsin D in different cell types of the rat liver. 644 77