You searched for: Enzymes

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Carbonic Anhydrase (CA) XII, also known as Car12 and CA12, is an extracellular enzyme involved in the regulation of the microenvironment acidity and tumour malignant phenotype, was originally identified as a protein overexpressed in some types of cancers. It has showed that CA XII is induced by hypoxia and oestrogen and expressed at high levels on various types of cancer. The enzyme is directly involved in tumour progression, and its inhibition has an anti-tumour effect. Apart from its role in carcinogenesis, the enzyme contributes to various other diseases like glaucoma and arteriosclerotic plaques, among others. CA XII is therefore regarded as promising target for specific therapies, and may be used as a novel prognostic marker in combination with histologic grade of the tumours.

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NAD Kinase (NADK) is an enzyme that belongs to the NAD Kinase family. It is a widely expressed enzyme, but it is not detected in skeletal muscle. NADK converts Nicotinamide Adenine Dinucleotide (NAD+) into NADP+, through phosphorylating the NAD+ coenzyme. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined.

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Phosphoserine phosphatase (PSP) is an enzyme that belongs to the serB family. PSPH catalyses magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Deficiency of this protein is thought to be linked to Williams syndrome. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.

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Cellulase (Onozuka R-10) is a multi-component enzyme system derived from Trichoderma viride and contains cellulase, alpha-amylase, hemicellulase, pectinase and protease activities.

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalyzing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It was shown to be induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation and is involved in biological processes like stress response and sporulation resulting in formation of a cellular spore. Catalytic activity: ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+

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Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.

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Fructose Bisphosphate Aldolase A (ALDOA) belongs to the class I fructose-bisphosphate aldolase family. ALDOA is a glycolytic enzyme that catalyses the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, Aldolase A in muscle, Aldolase B in liver and aldolase C in brain. Aldolase A Interacts with SNX9 and WAS. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. In addition, Aldolase A plays an important role in glycolysis and gluconeogenesis; it may also act as a scaffolding protein.

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Biotinylated Thrombin has covalently attached biotin for easy removal of the enzyme from cleavage reactions using immobilised streptavidin. This preparation is tested for activity using the same assay as for unmodified thrombin, and for >99% binding to streptavidin agarose.

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalysing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It can use both glutamine or ammonia as a nitrogen source. Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H₂O = AMP + diphosphate + NAD+ + L-glutamate.

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Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes. CAs form a family of enzymes that catalyse the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs rather slowly in the absence of a catalyst. One of the functions of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. The active site of most carbonic anhydrases contains a zinc ion. They are, therefore, classified as metalloenzymes. There are at least five distinct CA families (α, β, γ, δ and ε). These families have no significant amino acid sequence similarity and in most cases are thought to be an example of convergent evolution. The α-CAs are found in humans.
Carbonic anhydrase II (CA2) is also known as Carbonate dehydratase II, Carbonic anhydrase C, is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.

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Arylsulfatase A (ARSA) is a lysosomal enzyme that breaks down Cerebroside 3-Sulfate, a major constituent of the myelin sheet, into Cerebroside and Sulfate. The ARSA deficiency results in Metachromatic Leukodystrophy (MLD), a lysosomal storage disease in the central and peripheral nervous systems with severe and progressive neurological symptoms. Recombinant Human ARSA corresponds to the ARSA mature peptide and has sulfatase activity.

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Protein-glutamine gamma-glutamyltransferase 2 (TGM2) is a 78-kDa, calcium dependent enzyme,It belongs to the transglutaminase superfamily and transglutaminase family. The protein encoded by this TGM2 gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. TGM2 is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.

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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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Bile Salt Sulfotransferase (SULT2A1( is a cytosolic enzyme that belongs to the Sulfotransferase 1 family. SULT2A1 is primarily expressed in the liver and adrenal tissues, and to a lesser extent in the kidney. SULT2A1 utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor, and it catalyse the sulfonation of steroids and bile acids in the liver and adrenal glands. SULT2A1 may have a role in the inherited adrenal androgen excess.

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Selenocysteine Lyase belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Selenocysteine Lyase exists as a homodimer in the cytosol. In the brain, Selenocysteine Lyase is as an enzyme that putatively salvages Sec and recycles the selenium for selenoprotein translation. Selenocysteine Lyase catalyses the decomposition of L-selenocysteine to L-alanine and elemental selenium. Selenocysteine Lyase can be up-regulated In acute glomerulonephritis, it can also be regulated by JUN/AP-1.

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Sialic Acid Synthase (NANS) is an enzyme that contains one AFP-like domain. NANS is ubiquitous and plays a role in the biosynthetic pathways of sialic acids. NANS produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). It also can use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

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Galactose Mutarotase (GALM) is a cytoplasmic enzyme that belongs to the Aldose Epimerase family. GALM is a Mutarotase that converts alpha-Aldose to the beta -Anomer. GALM is active on D-Glucose, L-Arabinose, D-Xylose, D-Galactose, Maltose and Lactose. GALM may be required for normal Galactose metabolism by maintaining the equilibrium of alpha- and beta - anomers of Galactose.

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Carboxypeptidase B1 is an exopeptidase which specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. Expressed mainly in pancreas, CPB1 is a useful serum marker for acute pancreatitis and pancreatic graft rejection.Human CPB1 consists of a signal peptide, a pro region, and a mature chain. The purified rhCPB1 corresponds to the pro form, which can be activated by trypsin, the only pancreatic protease capable of generating active enzyme from the zymogen in vitro.

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Human N-Glycosylase/DNA Lyase is a DNA repair enzyme, which incises DNA at 8-oxoG residues, and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damage DNA. DGG1 has a beta -lyase activity that nicks DNA 3’ to the lesion.

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Sulfotransferase 1A2 (SULT1A2) is a member of the Sulfotransferase 1 family. Sulfotransferase enzymes catalyse the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 is a cytoplasmic protein and exists as a homodimer. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

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Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyses the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.

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The 3-hydroxykynurenine transaminase (3-HKT) gene plays a vital role in the development of malaria parasites by participating in the synthesis of xanthurenic acid, which is involved in the exflagellation of microgametocytes in the midgut of malaria vector species. The 3-HKT enzyme is involved in the tryptophan metabolism of Anophelines. The gene had been studied in the important global malaria vector, Anopheles gambiae.

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5-formyltetrahydrofolate cyclo-ligase (MTHFS) belongs to the 5-formyltetrahydrofolate cyclo-ligase family. It is an enzyme that catalyses the conversion of 5-formyltetrahydrofolate to 5,10-methenyltetrahydrofolate, contributes to tetrahydrofolate metabolism. MTHFS helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. An increased activity of the encoded protein can result in an increased folate turnover rate and folate depletion.

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Lipase family. The gene encoding this protein is expressed mainly in brain, liver and testes,followed by secreting into plasma and cerebral spinal fluid. The esterification of cholesterol is required for cholesterol transport. LCAT is a central enzyme in the extracellular metabolism of plasma lipoproteins. Defects in LCAT are the cause of lecithin-cholesterol acyltransferase deficiency (LCATD) and a cause of fish-eye disease (FED).

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ACAT2 is a cytoplasmic enzyme which belongs to the thiolase family. ACAT2 takes part in lipid metabolism, lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. It is responsible for the synthesis of cholesteryl esters which are part of lipoproteins containing apoB. ACAT2 deficiency contributes to severe mental retardation and hypotonus.

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Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localised to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.

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Phosphinothricin N-acetyltransferase (PAT) is an enzyme that acetylates the free NH2 group of L-phosphinothricin (L-PPT) in the presence of acetyl-CoA as a co-substrate. It is highly specific for L-PPT and does not acetylate other L-amino acids or structurally similar molecules. L-PPT is a glutamate analog that can inhibit glutamine synthetase activity in plants, resulting in the accumulation of ammonia to toxic levels and impairment of photosynthesis. The introduction of a PAT gene into a plant genome can confer resistance to glufosinate herbicide during post-emergent applications.

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Dipeptidase 1 (DPEP1) is a kidney membrane enzyme that belongs to the peptidase M19 family. DPEP1 is a homodimer and is inhibited by L-penicillamine. DPEP1 hydrolyses a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates. DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem. DPEP1 may play an important role in the regulation of leukotriene activity. DPEP1 expression in cancer is significantly higher than that in normal tissue. However, DPEP1 expression decreased with pathological differentiation, lymph-node and distant metastasis.

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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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Caspase 14 (CASP14) is an enzyme that belongs to the peptidase C14A family. The Caspase 14 protein is complexed of unprocessed caspase-14 and processed 19 kDa (p19) and 10 kDa (p10) subunits. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes, which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerise to form the active enzyme. CASP14 has been shown to be processed and activated by Caspase 8 and Caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier. It is believed to be a non-apoptotic caspase which is involved in epidermal differentiation, keratinocyte differentiation and cornification. CASP14 probably regulates maturation of the epidermis by proteolytically processing filaggrin.