Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.
Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues.
Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues.
Glycogen synthase kinase-3 is a serine-threonine protein kinase involved in regulation of metabolic enzymes such as glycogen synthase and ATP-Citrate lyase, and of protein phosphatase-1. It also phosphorylates brain tau-proteins, inducing an Alzheimer-like state, and protooncogene transcription factors. GSK-3β is one of two isozymes.
In enzymology, a nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction:a dinucleotide + H22 mononucleotides. Thus, the two substrates of this enzyme are dinucleotide and H2O, whereas its product is mononucleotide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. This enzyme participates in 5 metabolic pathways:purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis.
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The enzyme is inactivated with sulfhydryl reagents such as p-chloro-mercuribenzene sulfonic acid and transition metals such as Mn2+ or Zn2+. The enzyme is also inhibited with 1 mM EDTA. In a highly purified form, O-Glycanase adsorbs to glass surfaces and is inactivated or gives variable activities. Assays with purified substrates should be carried out in polypropylene vessels, and transfer of the enzyme solutions with glass pipettes should be avoided. The purified enzyme, as formulated, is stable at 2-8°C but about 30% of its activity is lost with a single freeze-thaw cycle. The enzyme activity is not significantly affected if the material is stored at room temperature for 24 hours. The optimum buffer for enzyme activity with the standard substrate is 50 mM sodium phosphate (pH 5.0). If glycosidase treatment is performed at suboptimal pH because of glycoprotein solubility or activity requirements, expect some diminution in enzyme activity.
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