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)

The rate of the reaction catalyzed by UDP-N-acetylglucosamine (GlcNAc):dolichol phosphate GlcNAc-1-phosphate transferase in rat liver endoplasmic reticulum vesicles was shown to be influenced by particular lipids. Utilizing in vitro assay conditions where the membrane vesicles retained latency of glucose-6-phosphatase activity, the addition of phosphatidylethanolamine, cardiolipin, or monogalactosyldiglyceride resulted in severalfold increases in the rate of dolichol pyrophosphate N-acetylglucosamine synthesis. Other phospholipids were not stimulatory. These rates were dependent on the concentrations of the exogenous lipids and of the substrate dolichol phosphate. In the presence of cardiolipin, the membrane-bound enzyme became more susceptible to inactivation by protease K and to inhibition by tunicamycin. Titration of cardiolipin-containing endoplasmic reticulum vesicles with adriamycin indicated that the majority of the cardiolipin was exposed on the outer surface. These results suggest that the particular lipids altered membrane structure in a way that allowed further access of the enzyme to substrate, inhibitor, and other molecules. Lipids observed in these studies to be stimulatory are known to exist in the macromolecular hexagonal phase and may therefore be affecting the GlcNAc-1-phosphate transferase by locally disrupting the bilayer structure of the membrane. As other dolichol-utilizing enzymes have been previously observed by other investigators to be similarly influenced by such lipids, the effects may be common to enzymes of the dolichol cycle.
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PMID:Specific lipids enhance the activity of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase in rat liver endoplasmic reticulum membrane vesicles. 165 76

We have studied the effects of prochlorperazine on the activities of UDP-glucuronosyltransferase and glucose-6-phosphatase (glucose-6-P'ase) in rat liver microsomes. The activity of UDP-glucuronosyltransferase was increased in a graded fashion by addition of prochlorperazine. Maximal stimulation occurred at 1 mg prochlorperazine to 2 mg microsomal protein, which resulted in a 6-fold increase in activity. However, with smaller concentrations of drug, there was a time-dependent increase in the activity of UDP-glucuronosyltransferase. Sensitivity of UDP-glucuronosyltransferase to activation by UDP-N-acetylglucosamine was lost after treatment of microsomes with prochlorperazine. These results indicate that prochlorperazine causes a profound reorganization of the interactions between lipids and enzyme since the activity and allosteric properties of UDP-glucuronosyltransferase are known to depend on interactions with lipids in a gel phase. Glucose-6-P'ase also was activated in a graded fashion by prochlorperazine; 1 mg of drug/2 mg microsomal protein resulted in a 60% increase in activity. The temperature-dependent instability of glucose-6-P'ase was increased by treatment of microsomes with prochlorperazine and could be prevented only partially by substrate. We conclude that prochlorperazine disrupts the structural organization between lipids and proteins in microsomal membranes, altering thereby the activity and regulation of at least two different integral membrane proteins.
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PMID:Effects of prochlorperazine on the function of integral membrane proteins. 283 74

The in vitro activities of glucose-6-phosphatase (G6P), UDP-glucuronyl transferase (GT) and P-450 were measured in liver homogenate and/or microsomal suspensions from puppies, 0-42 days of age (n = 26), and adult dogs (n = 3). For each of these enzymes, an age-related increase in the in vitro activity was observed, with the lowest value detected at birth. By the 28th-42nd day of postnatal life, P-450-specific activity was 350 and 85%, G6P 225 and 188%, p-nitrophenol GT 430 and 105% and bilirubin GT 317 and 123% of that seen in 0-hour-old puppies and adults dogs, respectively. The age-related changes in G6P and GT were observed when native enzymes or enzymes activated by deoxycholate or UDP-N-acetylglucosamine (GT) were used. However, the ratio between activated and native p-nitrophenol GT activity decreased as a function of age, and UDP-N-acetylglucosamine failed to activate bilirubin GT in puppies of 0-42 days of age. Total liver protein also increased with age, and hepatic water content was significantly higher in 0- to 42-day-old puppies (76.3%) than in adult dogs (71.4%). Thus, differences between puppies and adult animals were not the same when protein content or enzyme activities were expressed per unit of wet or dried liver weight. Phenobarbital, injected intraperitoneally at 15 mg/kg/day for 6 consecutive days to 8- to 13-day-old puppies (n = 3), produced induction of P-450 (235% of age-matched controls) and bilirubin GT activity (160%), diminished G6P activity (81%), and failed to modify p-nitrophenol GT activity (102%). These studies indicate that, in the puppy, (1) the in vitro activities of P-450, G6P and GT are immature at birth and develop during postnatal life; (2) as in other species, bilirubin and p-nitrophenol may be conjugated in the dog liver by two functionally distinct GT.
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PMID:Postnatal changes in hepatic microsomal enzyme activities in the puppy. 298 54

Effects of exercise regimens on the enzyme histochemical changes of articular chondrocytes of the humeral heads in adult shepherd-type dogs were studied. One group of 4 dogs was exercised by walking on a flat surface 5 days a week for 6 months. A 2nd group of 4 dogs was exercised under the same conditions, except that the dogs were forced to walk over platforms placed in their path. Three control dogs were exercised ad libitum in their housing area. In all dogs, the reactivity of lactic acid dehydrogenase was quite strong nicotinamide dinucleotide dehydrogenase was moderate, and glucose-6-phosphatase was week. Succinic acid dehydrogenase uridine diphosphate (UDP)-galactose-4-epimerase, and UDP-N-acetylglucosamine-4-epimerase were of weakly moderate staining reactivity. Consistent regional or laminar variability was not found among the chondrocytic populations of the exercised and control groups for the reactivity of the enzymes studied. However, regional and/or laminar variabilities in individuals of the experimental groups were identified. The weak reactivity of glucose-6-phosphatase as seemingly contradictory to the presence of intracellular lipids of adult articular chondrocytes. Lipid synthesis was suggested as a mechanism to store excessive quantities of hydrogen ions in an innocuous form, rather than in the potentially deleterious by-product of anaerobic glycolysis, lactic acid.
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PMID:Effects of exercise on the histochemical changes of articular chondrocytes in adult dogs. 680 69

Plasma membranes have been isolated from chicken liver and from Mc-29 virus induced transplantable hepatoma. The purity of membrane preparations has been checked by electron microscopy and by determination of the activity of some enzymes: 5'-nucleotidase, Na+, K+-ATP-ase, Mg2+-ATP-ase, alkaline beta-glycerophosphatase and glucose-6-phosphatase. In hepatoma membranes the activity of 5'-nucleotidase, Na+, K+-ATP-ase and Mg2+-ATP-ase was lower, that of alkaline phosphatase higher, than in liver membrane preparation. The incorporation rate of glucosamine-14C into UDP-N-acetylglucosamine and into plasma membrane glucosamine have been studied as well. The rate of synthesis of UDP-N-acetylglucosamine was faster in liver than in tumor cells. The labeling of hepatoma plasma membranes with glucosamine-14C occurred more slowly than that of liver ones. The rate of transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to membrane-bound glucosamine is lower in hepatoma, than in liver cells.
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PMID:Isolation and partial characterization of plasma membranes from chicken liver and from Mc-29 virus induced transplantable hepatoma. 745 56

Adult rat testis homogenates were fractionated by differential centrifugation followed by two discontinuous gradient centrifugation steps under identical conditions except for the absence of digitonin in the first gradient and the presence of 0.03% digitonin in the second gradient. The first gradient centrifugation yielded a membrane fraction enriched 28.8-fold in 5'-nucleotidase, 21.5-fold in UDP-Gal:GlcNAc galactosyltransferase and 18.6-fold in UDP-GlcNAc:alpha-D-mannoside N-acetylglucosaminyltransferase. Repeat centrifugation of this membrane fraction in the denser level of the gradient; this material was enriched 32.1-fold in 5'-nucleotidase but only 1.9-fold in galactosyltransferase and 8.4-fold in N-acetylglucosaminyltransferase. The plasma membrane fraction was shown to be free of glucose-6-phosphatase, succinate dehydrogenase, beta-N-acetylglucosaminidase, DNA, and RNA. The fraction therefore appears to be enriched in plasma membrane but relatively free of Golgi membrane contamination, as indicated by the relatively low levels of glycosyltransferases, and of contamination by other organelles. The testicular cells which contribute plasma membrane to this fraction have not yet been definitively identified; the contribution by Sertoli cells is particularly difficult to assess since these cells have been reported to be enriched in 5'-nucleotidase. However, sulfogalactosylalkylacylglycerol (SGG), a lipid previously shown to be present primarily in primary spermatocytes, spermatids, and spermatozoa, was enriched 33.1-fold in the plasma membrane fraction; this finding as well as experiments with [35S]sulfate-labeled sulfogalactosylalkylacylglycerol at various times after injection of radioactive label have indicated that both spermatocytes and spermatids were contributing SGG-rich membrane material to our plasma membrane preparation. This membrane material is most probably derived from the plasma membranes of the spermatocytes and spermatids.
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PMID:Enrichment of sulfogalactosylalkylacylglycerol in a plasma membrane fraction from adult rat testis. 745 82

Glycoprotein processing in Dictyostelium discoideum is characterized by enzyme catalyzed steps not reported in other organisms. One of these is the formation of a beta 1 --> 4 linkage between GlcNAc and the mannose linked to the core mannose in the alpha 1 --> 6 position of N-glycosides. A simple and sensitive assay for this GlcNAc transferase activity, using a tri-mannose acceptor and a low concentration of UDP-GlcNAc, was developed. Homogenates of the organism were subjected to sub-cellular fractionation by centrifugation in discontinuous sucrose gradients. The specific activity was enriched 4-5-fold in a crude membrane fraction. The transferase was purified 10-12-fold in a membrane fraction that bands on top of 1.1 M sucrose. This fraction was also enriched in nucleotidyldiphosphatase. The enriched fraction was deficient in glucose-6-phosphatase, an endoplasmic reticulum marker. Approx. 80% of the transferase activity was latent, and unavailable to protease. Purified membranes were either subjected to phase separation in Triton X-114, or sodium carbonate extraction or sonication. In each case, the transferase behaved as an intrinsic membrane protein. Several secreted and lysosomal proteins are modified by the enzyme. These data support the idea that the GlcNAc transferase is present as an integral Golgi membrane protein and that at least the catalytic center of the transferase is on the lumenal side of the vesicles.
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PMID:Subcellular distribution of "intersecting' beta-N-acetylglucosaminyltransferase in Dictyostelium discoideum. A likely marker for the Golgi apparatus. 865 99