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.
Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.
Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000.
This enzyme is a membrane protein and goes through an intermediate stage during the reaction where it is autophosphorylated with a phosphate group covalently linked to a basic amino acyl residue through an n-p bond.
Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry.
Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family.
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).
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).
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.
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.
Mutations of the cytosolic IDH 1 are a common feature in primary human brain cancers. Arginine 132 (R132) of IDH is highly conserved among different isoforms of IDH and is most commonly mutated to Histidine. Mutation of IDH1 R132H leads to accumulation of R(-)-2-hydroxyglutarate (2HG), which correlates with an increased risk for malignant brain tumors.
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.
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.
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.
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.
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- is one of two isozymes.
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.
In enzymology, an acylglycerol lipase (EC 3.1.1.23) is an enzyme that catalyzes a chemical reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism.
In enzymology, an acylglycerol lipase (EC 3.1.1.23) is an enzyme that catalyzes a chemical reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism.
The absence of exoglycosidase contaminants was confirmed by extended incubations with the corresponding pNP or MU-glycosides. No protease activity was detectable after incubation of the enzyme with 0.2 mg resorufin-labeled casein for ~18 hours at 37C according to the method described by Twining.
In enzymology, a nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction:a dinucleotide + H2O2 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.
In enzymology, a dTMP kinase (EC 2.7.4.9) is an enzyme that catalyzes the chemical reaction: ATP + dTMP rightleftharpoons ADP + dTDP. Thus, the two substrates of this enzyme are ATP and dTMP, whereas its two products are ADP and dTDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in pyrimidine metabolism.
In enzymology, a dtmp kinase (ec 2.7.4.9) is an enzyme that catalyzes the chemical reaction: atp + dtmp rightleftharpoons adp + dtdp. Thus, the two substrates of this enzyme are atp and dtmp, whereas its two products are adp and dtdp. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in pyrimidine metabolism.
The Casein kinase 1 family of protein kinases are serine/threonine-selective enzymes that function as regulators of signal transduction pathways in most eukaryotic cell types. CK1 isoforms are involved in Wnt signaling, circadian rhythms, nucleo-cytoplasmic shuttling of transcription factors, DNA repair, and DNA transcription.
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.
