You searched for: Enzymes

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Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH/MDH superfamily. MDH type 1 family. MDH2 catalyses the reversible oxidation of malate to oxaloacetate, utilising the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localised to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.

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LTA4H, which is short for Leukotriene A-4 hydrolase, is a 611 aa. protein. It belongs to the peptidase M1 family, and exists in cytoplasm. This protein has at least 4 isforms produced by alternative splicing, and two of them are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts. LTA4H involves in lipid metabolism and leukotriene B4 biosynthesis. It is a epoxide hydrolase that catalyses the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. It also has aminopeptidase activity.

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The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. It is thought that membrane-associated CPE acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway. Defects in this protein are implicated in type II diabetes due to impaired glucose clearance and insulin resistance.

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Mouse carboxypeptidase A2(CPA2) is a secreted pancreatic procarboxy -peptidase which belongs to the peptidase M14 family. CPA2 consists of a signal peptide, a pro region and a mature chain. It can be activated after cleavage of the pro peptide. CPA2 cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan.

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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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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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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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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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N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family. N-Acetylglucosamine-6-Sulfatase is required for the lysosomal degradation of the Glycosaminoglycans (GAG) Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase hydrolyses the 6-Sulfate groups of the N-Acetyl-D-Glucosamine 6-Sulfate units of Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase binds 1 Calcium ion per subunit. N-Acetylglucosamine-6-Sulfatase deficiency are the cause of Mucopolysaccharidosis Type 3D (MPS3D), an inborn error leading to lysosomal accumulation of heparan sulfate. MPS3D has profound mental deterioration, hyperactivity, and relatively mild somatic manifestations.

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Human nicotinate phosphoribosyltransferase (NAPRTase) is localised in the cytoplasm and is involved in biological processes such as NAD biosynthetic and metabolic processes, nicotinamide metabolic process, nicotinate nucleotide salvage, response to oxidative stress and water-soluble vitamin metabolic process. It functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN) and is essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. It is a crucial factor in the NAD+ biosynthesis pathway. Catalytic activity: Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.

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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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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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Isopentenyl Pyrophosphate Isomerase 2 (IDI2) belongs to the IPP isomerase type 1 family. Both isozymes, IDI1 and IDI2 are localised to the peroxisome by a PTS1-dependent pathway. IDI2 is expressed in skeletal muscle, which contains one nudix hydrolase domain. IDI2 binds one magnesium per subunit. IDI2 catalyses the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). It is reported that IDI2 is regulated independently from IDI1, by a mechanism that may involve PPAR- alpha.

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Calcium/Calmodulin-Dependent Protein Kinase Type 1 (CAMK1) belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family, and CaMK subfamily. CAMK1 contains one protein kinase domain and widely expressed. CAMK1 is phosphorylated by CaMKK1 and CaMKK2 on Thr-177. CAMK1 regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organisation, and neurite outgrowth. CAMK1 plays a role in K+ and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex.

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Carboxypeptidase A4 (CPA4) is a member of the peptidase M14 family. CPA4 is metalloprotease that could be involved in the histone hyperacetylation pathway. CPA4 binds one zinc ion per subunit and could catalyse to release of a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val.They have distinct expression patterns and different specificities for example, preferentially cleaving aromatic (carboxypeptidase As) or basic (carboxypeptidase Bs) residues. Several, such as carboxypeptidase Xs, have lost their catalytic activity. Carboxypeptidases play important roles in digestion of food, processing of bioactive peptides and blood coagulation.

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Human Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3) is an enzyme that in humans is encoded by the B3GAT3 gene, belongs to the glycosyltransferase 43 family. B3GAT3 is involved in a number of biological processes such as catalyzing the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans, forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate, gGlycosaminoglycans biosynthesis, transfering a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.It also plays a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins , hows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc and stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation.

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Acid sphingomyelinase-like phosphodiesterase 3a (SMPDL3A ) is a novel liver X receptor (LXR) -regulated gene, with an LXR response element within its promoter. The induction of SMPDL3A is LXR-dependent and is restricted to human blood cells with no induction observed in mouse cellular systems. LXR function as physiological sensors of cholesterol metabolites (oxysterols), regulating key genes involved in cholesterol and lipid metabolism. LXRs have been extensively studied in both human and rodent cell systems, revealing their potential therapeutic value in the contexts of atherosclerosis and inflammatory diseases.

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Carbonic Anhydrase 14 (CA14) belongs to the Alpha-Carbonic Anhydrase family. It is highly expressed in all parts of the central nervous system and lowly expressed in adult liver, heart, small intestine, colon, kidney, urinary bladder, and skeletal muscle. CA14 along with other Carbonic Anhydrases (CAs) participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA14 is predicted to be a type I membrane protein and catalyses the reversible hydration of carbon dioxide.

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NAD kinase catalyses the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. NAD kinase from Bacillus subtilis is not ATP-dependent but has a broader substrate specificity than human NAD kinase. It can economically produce NADP+ by using other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Catalytic activity: ATP + NAD+ = ADP + NADP+.

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Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyses the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.

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Sentrin-Specific Protease 7 (SENP7) acts as a SUMO-2/3-specific protease. SENP7 is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo. SENP7 has a restricted substrate specificity, and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 depolymerised poly-SUMO-2 chains but does not have activity against poly-SUMO-1 chains. SENP7 also had isopeptidase activity against di-SUMO-2- and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1.