You searched for: Enzymes

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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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Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family. QPRT plays an improtant role in catabolism of quinolinate which acts as a potent endogenous exitotoxin to neurons. In addition, QPRT serves as an an intermediate in the Tryptophan-Nicotinamide Adenine Dinucleotide pathway. QPRT participates in some pathways including Cofactor biosynthesis, NAD(+) biosynthesis and the Nicotinate D-Ribonucleotide from Quinolinate. In addition, QPRT is involved in the catabolism of Quinolinic Acid (QA). The activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.

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Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.

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Mouse Carboxylesterases 3 (CES3) is a member of five families of mammalian carboxylesterases that plays a role in catalysing hydrolytic and transesterification reactions with xenobiotics, anticancer pro-drugs and narcotics, and detoxifying organophosphates and insecticides. Mammalian carboxylesterases are enzymes with broad substrate specificities ranging from small molecule esters to longchain fatty acid esters. It is shown that CESs has key roles in the metabolism of a wide variety of clinical drugs, illicit narcotics and chemical nerve agents. CES3 is broadly expressed in liver, colon and brain.

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Kidney-Type Arginase (ARG2) is a member of the arginase family. Arginase is a manganese-containing enzyme which catalyses the hydrolysis of arginine to ornithine and urea. ARG2 is highly expressed in kidney and prostate, not founded in the liver, heart and pancreas. ARG2 has been implicated in the regulation of the arginine/ornithine concentrations in the cell. ARG2 may take part in the regulation of extra-urea cycle arginine metabolism and in down-regulation of nitric oxide synthesis. The extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase.

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Kynurenine aminotransferases (KATs) are pyridoxal-5’-phosphate-dependent enzymes that catalyse the conversion of L-kynurenine into kynurenic acid, a neuroactive metabolite whose unbalancing is associated with a number of brain disorders. Biochemical and structural investigations revealed that L-kynurenine (L-KYN) recognition by hKAT II is achieved by exploiting structural features that are peculiar of this isoform, thus offering the possibility to select/design inhibitor molecules specifically targeting hKAT II to be used as modulators of kynurenic acid synthesis in the CNS. hKAT II is one of the aminotransferases involved in the pyridoxal 5'-phosphate (PLP)-dependent irreversible transamination of L-kynurenine (L-KYN) to kynurenic acid (KYNA) in the central nervous system. When assayed in vitro the protein also displays beta-elimination activity.

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Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E.

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Fig tree Ficin (from Latex)

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Caspase-10 (CASP10) is a 521 amino acid protein member of the Cysteine-Aspartic Acid Protease (Caspase) family. CASP10 contains two DED (Death Effector) domains and is detectable in most tissues. CASP10 cleavage by Granzyme B and autocatalytic activity generate the two active subunits: Caspase-10 subunit p23/17, Caspase-10 subunit p12. Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the execution-phase of cell apoptosis, the initiation and execution. Human caspases can be subdivided into three functional groups: cytokine activation (caspase-1, -4, -5, and -13), apoptosis initiation (caspase-2, -8, -9, -and -10), and apoptosis execution (caspase-3, -6, and -7). CASP10 cleaves and activates caspases 3 and 7, but itself is processed by caspase 8. Defects in CASP10 are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome.

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0,25% Trypsin in HBSS (Hank’s Balanced Salt Solution) without calcium and magnesium.

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0,05% Trypsin/0,53 mM EDTA in HBSS (Hank’s Balanced Salt Solution) with sodium bicarbonate, without calcium and magnesium.

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Human DNA polymerase beta is constitutively expressed in cells. It fills in gaps in DNA that are formed following base excision repair. The activity cannot be affected by Aphidicolin, which is an inhibitor of DNA polymerase beta .

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Thymidylate kinase (DTYMK) is a ubiquitous enzyme of about 25 kD which belongs to thymidylate kinase family. DTYMK is important in the dTTP synthesis pathway for DNA synthesis. It participated in the pyrimidine metabolism pathway and dTTP biosynthesis pathway. DTYMK catalyses the conversion of dTMP to dTDP and catalyses the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium. Structural and functional analyses suggest that the cDNA codes for authentic human dTMP kinase. The mRNA levels and enzyme activities corresponded to cell cycle progression and cell growth stages.

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MDP1, which is short for nesium-dependent phosphatase 1, is a 176 aa. protein. It has 3 forms by different alternative splicing. This protein belongs to the HAD-like hydrolase superfamily, and usually takes its function with Magnesium. It can be inhibited by vanadate and zinc, and slightly by calcium. MDP1 is a Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.

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ALPP is a membrane protein and exits as a homodimer. ALPP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It has been shown to play a role in a number of processes including cell signaling, long-term potentiation, and cell adhesion, however, the best known and most commonly studied role is implicated in Alzheimer's research.

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SWSAP1 is a nucleus ATPase protein, interacts with ZSWIM7 and forms a functional complex. The complexs involved in homologous recombination repair and stabilises each other. SWS1AP1 also interacts with RAD51, RAD51B, RAD51C, RAD51D and XRCC3. It involves in homologous recombination repair. ATPase is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). SWSAP1 has a DNA-binding activity which is independent of its ATPase activity.

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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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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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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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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.

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Peptidyl-Prolyl Cis-Trans Isomerase H (PPIH) belongs to the Cyclophilin-type PPIase family that accelerate the folding of proteins. PPIases can catalyze the cis-trans isomerisaion of Proline Imidic peptide bonds in oligopeptides. PPIH participates in pre-mRNA splicing. It is a specific component of the complex that includes pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. In addition, PPIH has PPIase activity and may play a role as a chaperone mediating the interactions between different proteins inside the spliceosome.

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Thermo Scientific dsDNase is an engineered shrimp DNase designed for rapid and safe removal of contaminating genomic DNA from RNA samples. It is an endonuclease that cleaves phosphodiester bonds in DNA to yield oligonucleotides with 5’-phosphate and 3’-hydroxyl termini. Highly specific activity towards double-stranded DNA ensures that RNA and single-stranded DNA, such as cDNA and primers are not cleaved. dsDNase is easily inactivated by moderate heat treatment (55 °C). These features make dsDNase an excellent choice for gDNA elimination prior reverse transcription. It allows for dramatically simplified workflow which combines genomic DNA elimination and cDNA synthesis into one-tube procedure.

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Carbonic Anhydrase 4 (CA4) belongs to the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Carbonic anhydrase 4 is a glycosylphosphatidyl-inositol-anchored membrane isozyme expressed on the luminal surfaces of pulmonary (and certain other) capillaries and proximal renal tubules. Carbonic anhydrase 4 may stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It may have a role in inherited renal abnormalities of bicarbonate transport. Furthermore, Carbonic anhydrase 4 is essential for acid overload removal from the retina and retina epithelium and acid release in the choriocapillaris.

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Mouse CD73 is a glycosyl phosphatidylinositol (GPI) anchored membrane protein that belongs to the 5'-nucleotidase family. CD73 is an ecto 5'Nucleotidase expressed by most cell types. CD73 hydrolyses extracellular nucleotides into membrane permeable nucleosides. CD73 is one of several enzymes responsible for the production of extracellular adenosine, a signalling molecule that is involved in responses to inflammation and tissue injury. CD73 is a lymphocyte maturation marker that has functions independent of its catalytic activity. CD73 is also a regulator of leukocyte extravasation, a function that requires its 5'Nucleotidase activity.CD73 has also been reported to regulate expression of pro-inflammatory molecules in mouse endothelium.

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Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyses the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

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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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Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults.

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X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyses the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.

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Ribonuclease Pancreatic is a secreted enzyme that belongs to the pancreatic ribonuclease family. RNASE1 is an endonuclease that cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. RNASE1 prefers poly(C) as a substrate and hydrolyses 2',3'-cyclic nucleotides, with a pH optimum near 8.0. RNASE1 acts on single stranded and double stranded RNA.

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Malate Dehydrogenase, Cytoplasmic (MDH1) is an enzyme which belongs to the MDH Type 2 sub-family of LDH/MDH superfamily. MDH1 is involved in the Citric Acid Cycle that catalyses the conversion of Malate into Oxaloacetate (using NAD+) and vice versa. MDH1 should not be confused with Malic Enzyme, which catalyses the conversion of Malate to Pyruvate, producing NADPH. MDH1 also participates in Gluconeogenesis, the synthesis of Glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by Pyruvate Carboxylase to form Pxaloacetate, a Citric Acid Cycle intermediate. In order to transport the Oxaloacetate out of the Mitochondria, Malate Dehydrogenase reduces it to Malate, and it then traverses the inner Mitochondrial membrane. Once in the cytosol, the Malate is oxidised back to Oxaloacetate by MDH1. Finally, Phosphoenol-Pyruvate Carboxy Kinase (PEPCK) converts Oxaloacetate to Phosphoenol Pyruvate.