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

The topography of phosphatidylcholine, phosphatidylethanolamine and triacylglycerol biosynthetic enzymes within the transverse plane of rat liver microsomes was investigated using two impermeant inhibitors, mercury-dextran and dextran-maleimide. Between 70 and 98% of the activities of fatty acid : CoA ligase (EC 6.2.1.3), sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15), phosphatidic acid phosphatase (EC 3.1.3.4), diacylglycerol acyltransferase (EC 2.3.1.20), diacylglycerol cholinephosphotransferase (EC 2.7.8.2) and diacylglycerol ethanolaminephosphotransferase (EC 2.7.8.1) were inactivated by mercury-dextran. Dextran-maleimide caused 52% inactivation of the sn-glycerol-3-phosphate acyltransferase. Inactivation of each of these activities except fatty acid : CoA ligase occurred in microsomal vesicles which remained intact as evidenced by the maintenance of highly latent mannose-6-phosphatase activity (EC 3.1.3.9). These glycerolipid biosynthetic activities were not latent, indicating that substrates have free access to the active sites. Moreover, ATP, CDP-choline and CMP appeared unable to penetrate the microsome membrane. These data indicate that the active sites of thease enzymes are located on the external surface of microsomal vesicles. It is concluded that the biosynthesis of phosphatidylcholine, phosphatidylethanolamine and triacylglycerol occurs asymmetrically on the cytoplasmic surface of the endoplasmic reticulum.
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PMID:Topography of phosphatidylcholine, phosphatidylethanolamine and triacylgycerol biosynthetic enzymes in rat liver microsomes. 615 20

Male mice of Kunming strain were infected with 10,000 tachyzoites intraperitoneally. 2 hours after infection the mice were divided into 2 groups and administered 5% of amylum and 200 mg/kg of artemether by gavage for 8 consecutive days. The ultrastructural enzyme cytochemical studies on cytidine monophosphatase (CMP-ase) and glucose-6-phosphatase (G-6-P-ase) of the parasites were carried out. CMP-ase was found scattered in the lysosomes of the parasites as well as in the macrophages. No differences were observed in the localization and intensity of CMP-ase activity between the nontreated and treated with drug parasites. G-6-P-ase was found surrounding the parasite membrane and scattered in the parasitophorous vacuole in the nontreated parasites. After treatment with artemether, the intensity of G-6-P-ase activity was decreased compared with nontreated control parasites. It is suggested that artemether may exert some action on the G-6-P-ase of T. gondii and thus influence the energy metabolis of the parasite.
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PMID:[Studies on the enzyme cytochemistry of Toxoplasma gondii and the influence of artemether]. 855 92