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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)

Sorbitol density gradient centrifugation applied to intestinal mucosa homogenates resulted in a complete separation of soluble calcium-binding protein from the bound fraction of calcium-binding protein, providing further documentation of the bound pool of calcium-binding protein. The peak of the bound calcium-binding protein was not associated with the major peaks of any of the markers used, but was associated with minor peaks of alkaline phosphatase, RNA, and glucose-6-phosphatase. Lack of association of bound calcium-binding protein with (Na+ + K+)-ATPase indicated that the bound calcium-binding protein is not on the basolateral membrane. Differential centrifugation fractionation indicated that the bound calcium-binding protein is not associated with nuclei or mitochondria. The bound calcium-binding protein also could not be detected in partially purified brush borders. Exclusion of the brush border and basolateral membranes as the location of the bound calcium-binding protein suggests an intracellular locale.
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PMID:Studies on the subcellular localization of the membrane-bound fraction of intestinal calcium-binding protein. 11 17

The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on glucose-6-phosphatase in the microsomes of rat liver was investigated. Addition of Ca2+ up to 2.5 microM to the enzyme reaction mixture caused a significant increase of glucose-6-phosphatase activity in hepatic microsomes, while Ni2+, Zn2+, Cd2+, Cu2+, Mn2+ and Co2+ (20 microM) did not have an appreciable effect. Vanadate (V5+) markedly inhibited the enzyme activity; a significant inhibitory effect was seen at 10 microM V5+. The Ca2+-induced increase of glucose-6-phosphatase activity was reversed by the presence of regucalcin; the effect was complete at 1.0 microM of the protein. Regucalcium had no effect on the basal activity of the enzyme. Meanwhile, the inhibitory effect of V5+ (10-100 microM) on glucose-6-phosphatase was not appreciably blocked by the presence of regucalcin (up to 2.0 microM). The present data suggest that hepatic microsomal glucose-6-phosphatase is uniquely regulated by Ca2+ and V5+, of various metals, and that the Ca2+ effect is reversed by regucalcin. The present study supports the view that regucalcin plays an important role as a regulatory protein in liver cell function related to Ca2+.
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PMID:Effects of Ca2+ and V5+ on glucose-6-phosphatase activity in rat liver microsomes: the Ca2+ effect is reversed by regucalcin. 254 64

Hepatic glucose-6-phosphatase (G-6-Pase) catalyses the terminal step of hepatic glucose production and it plays a key role in the maintenance of blood glucose homeostasis. Hepatic G-6-Pase is an integral resident endoplasmic reticulum (ER) protein and it is part of a multicomponent system. Its active site is situated inside the lumen of the ER and transport proteins are needed to allow its substrates, glucose-6-phosphate (G-6-P) (and pyrophosphate), and its products, phosphate and glucose to cross the ER membrane. In addition, a calcium-binding protein is also associated with the G-6-Pase enzyme. Recent immunological studies have shown that G-6-Pase (which has conventionally been thought to be present only in the gluconeogenic organs) is present in minor cell types in a variety of human tissues and that its distribution changes dramatically during human development. In all the tissues, enzymatic analysis, direct transport assays and/or immunological detection of the ER glucose and phosphate transport proteins have been used to demonstrate the presence and activity of the whole G-6-Pase system. The G-6-Pase protein is very hydrophobic and has proved difficult to purify to homogeneity. Four proteins of the system have now been isolated and polyclonal antibodies have been raised against them; two have also been cloned. The available sequences, together with topological studies, have given some information about both the topology of the proteins in the ER and the probable mechanisms by which the proteins are retained in the ER.
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PMID:Glucose-6-phosphatase proteins of the endoplasmic reticulum. 771 31