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)

It is established that in embryos incubated until the early blastula stage in the solution of insulin with addition of cycloheximide or puromycin, there is neither a decrease in the hexokinase and glucose-61 phosphate dehydrogenase activities nor an increase in the phosphofructokinase activity, as it is shown under the influence of insulin only. Puromycin removes an inhibitory effect of insulin on the glucose-6-phosphatase activity, and actinomycin D removes this influence with respect to glucose-6-phosphate dehydrogenase and glucose-6-phosphatase activities. The addition of antibiotics removes inhibition of the hexokinase, glucose-6-phosphate dehydrogenase and glucose-6-phosphatase activities by the hormone in the unfertilized eggs as well. Actinomycin D alone inhibits the hexokinase and activates the phosphofructokinase activities in the embryos and eggs, puromycin decreases their hexokinase activity and cycloheximide has the same effect on the glucose-6-phosphatase activity in the embryos only.
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PMID:[Effect of insulin on activity of carbohydrate metabolism enzymes in loach embryos in early development]. 19 74

Incubation of hepatocytes in the presence of microcystin-LR, okadaic acid, calyculin A (inhibitors of protein phosphatases PP1 and PP2A) or microcystin-RR (a specific inhibitor of PP2A) activated glucose-6-phosphatase both in the supernatant and in intact or disrupted microsomes. Puromycin, an inhibitor of protein synthesis, totally suppressed this activating effect, suggesting the involvement of protein phosphatases in the regulation of glucose-6-phosphatase synthesis.
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PMID:Inhibition of protein phosphatases activates glucose-6-phosphatase in isolated rat hepatocytes. 838 Jan 44

Contribution of translocon peptide channels to the permeation of low molecular mass anions was investigated in rat liver microsomes. Puromycin, which purges translocon pores of nascent polypeptides, creating additional empty pores, raised the microsomal uptake of radiolabeled UDP-glucuronic acid, while it did not increase the uptake of glucose-6-phosphate or glutathione. The role of translocon pores in the transport of small anions was also investigated by measuring the effect of puromycin on the activity of microsomal enzymes with intraluminal active sites. The mannose-6-phosphatase activity of glucose-6-phosphatase and the activity of UDP-glucuronosyltransferase were elevated upon addition of puromycin, but glucose-6-phosphatase and beta-glucuronidase activities were not changed. The increase in enzyme activities was due to a better access of the substrates to the luminal compartment rather than to activation of the enzymes. Antibody against Sec61 translocon component decreased the activity of UDP-glucuronosyltransferase and antagonized the effect of puromycin. Similarly, the addition of the puromycin antagonist anisomycin or treatments of microsomes, resulting in the release of attached ribosomes, prevented the puromycin-dependent increase in the activity. Mannose-6-phosphatase and UDP-glucuronosyltransferase activities of smooth microsomal vesicles showed higher basal latencies that were not affected by puromycin. In conclusion, translationally inactive, ribosome-bound translocons allow small anions to cross the endoplasmic reticulum membrane. This pathway can contribute to the nonspecific substrate supply of enzymes with intraluminal active centers.
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PMID:Translocon pores in the endoplasmic reticulum are permeable to small anions. 1661 37