The Lipid Dependence of Glucose-6-Phosphate Phosphohydrolase
نویسندگان
چکیده
منابع مشابه
Inhibitory effect of physiological bicarbonate ion levels on the activities of glucose 6-phosphate phosphohydrolase.
Rat liver microsomal glucose 6-phosphate phosphohydrolase has been shown to possess two further catalytic activities: the hydrolysis of inorganic pyrophosphate to orthophosphate and a pyrophosphate-glucose phosphotransferase activity. Physiological concentrations of bicarbonate ion (10 to 50 mM) have been found to inhibit all three activities. A detailed kinetic analysis of the nature and exten...
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Recent investigations supported the existence of 2 components of the endoplasmic reticulum participating in the process of glucose 6-phosphate hydrolysis: the glucose 6-phosphate-specific transporter that mediates the movement of the substrate from the cytoplasmic membrane surface into the lumen and the unspecific phosphohydrolase on the luminal side of the membrane [ 1,2]. However, this model ...
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The lung contains two distinct forms of phosphatidic acid phosphatase (PAP). PAP1 is a cytosolic enzyme that is activated through fatty acid-induced translocation to the endoplasmic reticulum, where it converts phosphatidic acid (PA) to diacylglycerol (DAG) for the biosynthesis of phospholipids and neutral lipids. PAP1 is Mg(2+) dependent and sulfhydryl reagent sensitive. PAP2 is a six-transmem...
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Lipid phosphate phosphohydrolase (LPP) has recently been proposed to have roles in signal transduction, acting sequentially to phospholipase D (PLD) and in attenuating the effects of phospholipid growth factors on cellular proliferation. In this study, LPP activity is reported to be enriched in lipid-rich signalling platforms isolated from rat lung tissue, isolated rat type II cells and type II...
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A new D-glucose-6-phosphate phosphohydrolase (G6Pase) inhibitor, CJ-21,164 (1) was isolated from the fermentation broth of the fungus Chloridium sp. CL48903. The structure was elucidated to be a novel tetramer of the salicylic acid derivatives by spectroscopic analyses. Compound I inhibited G6Pase in rat liver microsomes with an IC50 of 1.6 microM. Glucose output from hepatocytes isolated from ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1982
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(82)84591-8