You searched for: Enzymes

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Proteinase-3 is a neutral serine proteinase that belongs to the peptidase S1 family and Elastase subfamily. It contains one peptidase S1 domain and it is expressed mainly in neutrophil granulocytes. The primary function of Proteinase-3 is thought to be degradation of extracellular proteins at sites of inflammation, but excessive or prolonged proteolytic activity may cause harmful effects in the body. It is the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the cANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease Wegener's granulomatosis.

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Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyses the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.

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Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

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Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesised as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER , the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis.PCSK9 also plays a role in neural development.

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Glutamine Synthetase reglutes intracellular concentration of glutamate. Glutamine Synthetase catalyses the synthesis of glutamine from glutamate and ammonia. Glutamine is an important source of energy and that takes part in cell prolifetation, inhibition of apoptosis, and cell signaling. Glutamine Synthetase is expressed during early fetal stages, and has a role in maintaining body PH by removing ammonia from circulation. Mutations in the GLUL gene are related to congenital glutamine deficiency.

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Mouse Lactate dehydrogenase A (LDHA) is a member of the LDH/MDH superfamily and LDH family. LDHA catalyses the inter-conversion of pyruvate and L-lactate with concomitant inter-conversion of NADH and NAD+. LDHA is found in most somatic tissues, though predominantly in muscle tissue and tumours. It has also been shown that LDHA plays an important role in the development, invasion and metastasis of malignancies. Mutations in LDHA have been linked to exertional myoglobinuria.

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Pancreatic Lipase-Related Protein 2 (PNLIPRP2) is a secreted protein that belongs to the Lipase family of AB hydrolase superfamily. PNLIPRP2 is a lipase with broad substrate specificity that contains one PLAT domain. PNLIPRP2 is expressed mainly in pancreas. PNLIPRP2 can hydrolyse both phospholipids and galactolipids. PNLIPRP2 acts preferentially on monoglycerides, phospholipids and galactolipids. PNLIPRP2 also contributes to milk fat hydrolysis.

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Geranylgeranyl pyrophosphate synthase (GGPS1) is a member of the FPP/GGPP synthase family. GGPS1 is highly expressed in testis, heart and skeletal muscle. GGPS1 is localised in the cytoplasm and has geranylgeranyl diphosphate (GGPP) synthase activity. It catalyses the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. Other transcriptional splice variants have been found.

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GDP-L-Fucose Synthase is a NADP(H)-binding protein. It catalyses the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-dexoymannose to GDP-L-fucose. GDP-L-Fucose is the substrate of several fucosyltransferase, involving the expression of mamy glycoconjugates, including blood group ABH antigens and development adhesion antigens. Mutations in the TSTA3 gene may cause leukocyte adhesion deficiency type II.

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Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway, fatty acid metabolic process and lipid metabolic process.

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Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family. Phosphomannomutase 1 can catalyses the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose which required for a number of critical mannosyl transfer reactions. PMM1 is highly expressed in liver, heart, brain, and pancreas, but lower expression in skeletal muscle. In addition, PMM1 may be responsible for the degradation of glucose-1,6 bisphosphate in ischemic brain.

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CAMK1D is a serine/threonine kinase that is a member of the calcium/calmodulin-dependent protein kinase family. It contains a protein kinase domain. CAMK1D expressed in polymorphonuclear leukocytes and may be part of the chemokine signal transduction pathway that regulates granulocyte function. It may also be involved in modulation of neuronal apoptosis. It activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons.

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Catalase (CAT) is a member of the catalase family. It exists as a homotetramer that occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Catalase is localised in the peroxisome. Catalase promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells, and normal and transformed fibroblast cells. Defects in CAT are the cause of acatalasemia which is characterised by absence of catalase activity in red cells and is associated with ulcerating oral lesions.

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Ribulose-Phosphate 3-Epimerase (RPE) is a member of the Ribulose-Phosphate 3-Epimerase family. RPE exists as a homodimer and catalyses the reversible epimerisation of D-ribulose 5-phosphate to D-xylulose 5-phosphate. RPE binds one divalent metal cation per subunit and contains tightly bound Fe2+ when produced in E. coli, but the physiological cofactor may be Co2+, Mn2+ or Zn2+. It has been shown that RPE participates in 3 metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma. IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Protein Disulfide-Isomerase A4 (PDIA4) is an endoplasmic reticulum luminal protein that belongs to the protein disulfide isomerase family. Human PDIA4 is synthesised as a 625 amino acid precursor that contains a 20 amino acid signal sequence, and a 625 amino acid mature chain, including three thioredoxin domains. PDIA4 catalyses the rearrangement of -S-S- bonds in proteins and is thought to be a deoxycytidine kinase. In addition, PDIA4 serves as a proteases protein disulfide isomerase, phospholipase or an arrangement of these.

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Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily. PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.

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beta -1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and beta -N-Acetylglucosaminyl-Glycolipid beta -1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.

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Carnosine Dipeptidase 1 (CNDP1) belongs to the M20 metalloprotease family. CNDP1 is specifically expressed in the brain, serum and adult nervous central system. It is identified as human carnosinase. CNDP1 contains trinucleotide (CTG) repeat length polymorphism in the coding region and is inhibited by the metal chelator 1,10-o-phenantrolin. In addition, CNDP1 can hydrolyse the beta-Ala|-His dipeptide (carnosine), anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine. CNDP1 deficiency has been associated with homocarnosinosis disease.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Ribonuclease 3 (RNASE3) is a basic protein that is localised to the eosinophil primary matrix and belongs to the pancreatic ribonuclease family. RNASE3 is released during degranulation of eosinophils. RNASE3 possesses a wide variety of biological activities. RNASE3 interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). RNASE3 exhibits antibacterial activity, including cytoplasmic membrane depolarisation of preferentially Gram-negative, but also Gram-positive strains. It promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

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Deoxyuridine 5'-Triphosphate Nucleotidohydrolase Mitochondrial (dUTPase) belongs to the dUTPase family. dUTPase exits as a homotrimer and is involved in nucleotide metabolism. dUTPase produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. The dUTPase increase in PCR product yield, length and fidelity enables further down-stream applications. These effects make dUTPase useful in PCR fidelity and yield-sensitive applications. dUTPase is specific for dUTP and is critical for the fidelity of DNA replication and repair.

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Dipeptidyl peptidase 3(DPP3), is a member of the S9B family in clan SC of the serine proteases. DPP3 has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH). It releases an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity and also acts on dipeptidyl 2-naphthylamides.Increased activity of this protein has a relationship with endometrial and ovarian cancers.

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Chymotrypsin-Like Protease CTRL-1 is a protease that belongs to the peptidase S1 family. Human CTRL-1 is synthesised as a 264 amino acid (aa) precursor that contains an 18 aa signal sequence, 15 aa activation peptide and a 231 aa mature chain. CTRL-1 Contains 1 peptidase S1 domain. It has many molecular functions, such as hydrolase, protease, and serine protease. CTRL-1 plays a role in digest and hydrolyse proteins in biological process.

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Carbonic Anhydrase 7 (CA7) is a member of the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Furthermore, Alpha-carbonic anhydrase is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA7 is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine, but it is inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA) by saccharin and Foscarnet.

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Hyaluronidase-1 (HYAL1) is a secreted lysosomal hyaluronidase that belongs to the glycosyl hydrolase 56 family. HYAL1 contains one EGF-like domain and is highly expressed in the liver, kidney, and heart, but it is weakly expressed in the lung, placenta, and skeletal muscle. HYAL1 is thought to be involved in cell proliferation, migration, and differentiation. It may play a role in promoting tumor progression and blocking the TGFB1-enhanced cell growth. Mutations in HYAL1 are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency.

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Fructose-1,6-Bisphosphatase 1 (FBPase 1) is a member of the FBPase class 1 family. FBPase 1 is a gluconeogenesis regulatory protein, which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBPase 1 can assume an active R-state, or an inactive T-state. FBPase 1 deficiency is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis in newborn infants or young children. FBPase 1 coupled with phosphofructokinase (PFK) is involved in the metabolism of pancreatic islet cells.

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Pyruvate Kinase Isozymes R/L (PKLR) belongs to the pyruvate kinase family, There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver; R is found in red cells; M1 is the main form in muscle, heart and brain; M2 is found in early fetal tissues. PKLR exists as a homotetramer and catalyses the production of phosphoenolpyruvate from pyruvate and ATP. Defects in PKLR are also the cause of pyruvate kinase deficiency of red cells, which is a frequent cause of hereditary non-spherocytic hemolytic anemia.

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Phosphoglucomutase-2 (PGM2) is a member of PGM family, which catalyses the inter-conversion of sugar phosphates and participates in anabolic and catabolic reactions. When cells are grown in glucose, PGM catalyses the conversion of glucose-6-phosphate to glucose-1-phosphate an important precursor required for the synthesis of UDP glucose and trehalose. PGM2 catalyses the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses, and it may also catalyse the interconversion of glucose-1-phosphate and glucose-6-phosphate. But this protein has low glucose 1,6-bisphosphate synthase activity.