NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity.
NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity.
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Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site.
Keratan-sulfate endo-1,4-beta-galactosidase (EC 3.2.1.103, endo-beta-galactosidase, keratan sulfate endogalactosidase, keratanase, keratan-sulfate 1,4-beta-D-galactanohydrolase) is an enzyme with system name keratan-sulfate 4-beta-D-galactanohydrolase. This enzyme catalyses the following chemical reaction:Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate. Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl 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.
Factor V activator for RVV contains fucose, mannose, galactose, glucosamine, and neuraminic acid. Factor V activating enzyme from RVV is an arginine esterase that is sensitive to diisopropyl fluorophosphate (DFP).
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.
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.
Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate (aka glycerone phosphate, outdated) to sn-glycerol 3-phosphate. Glycerol-3-phosphate dehydrogenase serves as a major link between carbohydrate metabolism and lipid metabolism. It is also a major contributor of electrons to the electron transport chain in the mitochondria.
