EC Number |
Recommended Name |
Application |
---|
3.5.1.104 | peptidoglycan-N-acetylglucosamine deacetylase |
pharmacology |
studies on peptidoglycan modifications by Streptococcus pneumoniae |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
pharmacology |
the enzyme is a target for antibiotic therapy and structure-based drug design |
3.5.1.119 | Pup amidohydrolase |
pharmacology |
the enzyme provides an ideal target for the development of selective chemotherapies |
3.5.2.6 | beta-lactamase |
pharmacology |
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors |
3.5.3.1 | arginase |
pharmacology |
enzyme is a target for inhibitor design based on arginine analogues with uncharged, tetrahedral functional groups |
3.5.3.4 | allantoicase |
pharmacology |
possibility to develop metabolism-based strategies for mosquito control |
3.5.3.6 | arginine deiminase |
pharmacology |
ADI has anti-cancer activity by causing depletion of L-arginine, fusion of ADI to 20 kDa PEG improves its pharmaceutical efficiency by increasing the half-life of the enzyme in serum, clinical studies, overview |
3.5.3.6 | arginine deiminase |
pharmacology |
ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia, ADI in clinical studies, overview |
3.5.3.15 | protein-arginine deiminase |
pharmacology |
PAD1 is a target in skin diseases including psoriasis |
3.5.3.15 | protein-arginine deiminase |
pharmacology |
PAD2 is a target for treatment of glaucoma and multiple sclerosis |
3.5.3.15 | protein-arginine deiminase |
pharmacology |
PAD3 is a target in skin diseases including psoriasis, PAD3-like protein is a target for treatment of certain cancers |
3.5.3.15 | protein-arginine deiminase |
pharmacology |
PAD4 inhibitors F-and Cl-amidine represent potential lead compounds for the treatment of rheumatoid arthritis because a growing body of evidence supports a role for PAD4 in the onset and progression of this chronic autoimmune disorder |
3.5.4.1 | cytosine deaminase |
pharmacology |
exogenous cytosine deaminase gene expression in Bifidobacterium breve I-53-8w for tumor-targeting enzyme/prodrug therapy, overview |
3.5.4.1 | cytosine deaminase |
pharmacology |
the recombinant fusion enzyme HSV-1TKglyCD might be useful in cancer gene therapy |
3.5.4.1 | cytosine deaminase |
pharmacology |
applicability of gene-directed enzyme prodrug therapy (GDEPT), prodrug encapsulation in liposomes, liposomal 5-fluorocytosine (5-FC) achieves high local concentration for suicide therapy |
3.5.4.1 | cytosine deaminase |
pharmacology |
applicability of gene-directed enzyme prodrug therapy using the capability of human adipose tissue-derived mesenchymal stem cells (AT-MSC) as cellular vehicles expressing cytosine deaminase, CDy-AT-MSC/5FC-system, analyzed in cell lines and xenografts |
3.5.4.1 | cytosine deaminase |
pharmacology |
applicability of gene-directed enzyme prodrug therapy, feasibility of using magnetic resonance spectroscopy and optical imaging to measure non-invasively expression and function of cytosine deaminase in a preclinical tumor model |
3.5.4.1 | cytosine deaminase |
pharmacology |
cancer chemotherapy, antibody-directed enzyme-prodrug therapy (GDEPT/ADEPT), biopanning assay |
3.5.4.1 | cytosine deaminase |
pharmacology |
negative selection system for actinobacteria based on cytosine deaminase |
3.5.4.4 | adenosine deaminase |
pharmacology |
Plasmodium falciparum-specific inhibitors of adenosine deaminase have potential for development as antimalarials without inhibition of host enzyme |
3.5.4.12 | dCMP deaminase |
pharmacology |
elevated level of dCMPase in transformed cells and tumors: enzyme may represent another important target for cancer chemotherapy |
3.5.4.12 | dCMP deaminase |
pharmacology |
might have applications in cancer chemotherapy. Enzyme may be an inhibitor target for antitumor agents |
3.5.4.12 | dCMP deaminase |
pharmacology |
enzyme might be a reasonable target for chemotherapeutic agents directed against parasitic as well as neoplastic diseases by limiting the synthesis of dUMP, particularly when used in combination with inhibitors of dTMP synthase or other purine and pyrimidine inhibitors of DNA synthesis |
3.5.4.25 | GTP cyclohydrolase II |
pharmacology |
enzyme is a potential drug target, since numerous pathogenic microorganims are absolutely dependent on endogenous synthesis of riboflavin, target for development of bactericidal inhibitors |
3.6.1.5 | apyrase |
pharmacology |
the enzyme may serve as a therapeutic agent for inhibition of platelet-mediated thrombosis |
3.6.1.23 | dUTP diphosphatase |
pharmacology |
the enzyme is a chemotherapeutic target |
3.6.1.23 | dUTP diphosphatase |
pharmacology |
the enzyme is a potential target for antiviral drug design |
3.6.1.27 | undecaprenyl-diphosphate phosphatase |
pharmacology |
the enzyme is an attractive drug target since it is not used by humans |
3.6.2.1 | adenylylsulfatase |
pharmacology |
biological sulfation process |
3.6.4.B7 | RadA recombinase |
pharmacology |
application potential of archaeal nanobiomotors in drug delivery |
3.6.4.13 | RNA helicase |
pharmacology |
conservation of the NTP-binding pocket among viruses of the family Flaviviridae as potential for development of therapeutics |
3.6.4.13 | RNA helicase |
pharmacology |
peptide inhibitors reproducing the structure of the autoregulatory motif as possibility to develop effective antivirals |
3.6.5.2 | small monomeric GTPase |
pharmacology |
the enzyme is a pharmacological target for the treatment of cardiovascular diseases |
3.10.1.1 | N-sulfoglucosamine sulfohydrolase |
pharmacology |
early treatment of CNS lesions by adeno-associated virus-mediated intraventricular injection of both SGSH and SUMF1 genes may represent a feasible therapy for MPS-IIIA |
4.1.1.11 | aspartate 1-decarboxylase |
pharmacology |
Mycobacterium tuberculosis is the etiological agent of tuberculosis and PanD is a potential drug target |
4.1.1.15 | glutamate decarboxylase |
pharmacology |
the enzyme is a potential important marker for the prediction and diagnosis of type 1 diabetes, and for the development of antigen-specific therapies for the treatment of type 1 diabetes |
4.1.1.17 | ornithine decarboxylase |
pharmacology |
the enzyme is a target in the combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor MQT 1426, i.e. D-Lys-spermine, against murine squamous cell carcinoma, overview |
4.1.1.17 | ornithine decarboxylase |
pharmacology |
the enzyme ODC is possibly useful in chemotherapy of human malignancies, such as skin cancer |
4.1.1.17 | ornithine decarboxylase |
pharmacology |
ODC is a target for chemoprevention of apoptosis |
4.1.1.17 | ornithine decarboxylase |
pharmacology |
pharmacological inhibition of ODC is a promising therapeutic paradigm for the treatment of visceral and perhaps other forms of leishmaniasis |
4.1.1.23 | orotidine-5'-phosphate decarboxylase |
pharmacology |
human UMP synthase enzyme may be a potential cancer drug target |
4.1.1.25 | tyrosine decarboxylase |
pharmacology |
biosynthesis of pharmaceutically important monoterpenoid indole alkaloids |
4.1.1.28 | aromatic-L-amino-acid decarboxylase |
pharmacology |
biosynthesis of pharmaceutically important monoterpenoid indole alkaloids |
4.1.1.32 | phosphoenolpyruvate carboxykinase (GTP) |
pharmacology |
development of a PEPCK inhibitor may lead to a new therapeutic strategy for the treatment of type II diabetes |
4.1.1.32 | phosphoenolpyruvate carboxykinase (GTP) |
pharmacology |
orally active compounds reversibly inhibiting PEPCK improve glucose homeostasis in type 2 diabetics |
4.1.1.33 | diphosphomevalonate decarboxylase |
pharmacology |
the enzyme is an antibiotic target, since inhibition prevents the production of isopentenyl diphosphate |
4.1.1.50 | adenosylmethionine decarboxylase |
pharmacology |
the enzyme is a target for cancer chemotherapy |
4.1.1.50 | adenosylmethionine decarboxylase |
pharmacology |
potentially important drug target for the chemotherapy of proliferative and parasitic diseases |
4.1.1.50 | adenosylmethionine decarboxylase |
pharmacology |
potentially important target for chemotherapy of filiarial infection |
4.1.1.50 | adenosylmethionine decarboxylase |
pharmacology |
potential target for therapeutic agents against various parasitic diseases and proliferating disorders |
4.1.1.53 | phenylalanine decarboxylase |
pharmacology |
side-effects of pharmacologically active decarboxylation products considered |
4.1.2.9 | phosphoketolase |
pharmacology |
polyketide natural products play an important role in the treatment of a wide range of human physiological disorders |
4.1.2.10 | (R)-mandelonitrile lyase |
pharmacology |
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile |
4.1.2.10 | (R)-mandelonitrile lyase |
pharmacology |
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals |
4.1.2.25 | dihydroneopterin aldolase |
pharmacology |
the Fas multifunctional enzyme with the activity of the first three enzymes of the folate synthesis pathway: dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase is an attractive target for chemotherapy, sin |
4.1.2.42 | D-threonine aldolase |
pharmacology |
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization |
4.1.2.42 | D-threonine aldolase |
pharmacology |
the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals |
4.1.2.47 | (S)-hydroxynitrile lyase |
pharmacology |
enantiomerically pure cyanohydrins produced by enzyme-catalyzed synthesis are important synthetic intermediates for pharmaceuticals |
4.1.2.48 | low-specificity L-threonine aldolase |
pharmacology |
biotechnological potential for the syntheses of pharmaceutically relevant drug molecules because of the stereospecificity |
4.2.1.1 | carbonic anhydrase |
pharmacology |
extensively investigated enzyme as a target for drug design |
4.2.1.46 | dTDP-glucose 4,6-dehydratase |
pharmacology |
the enzyme is essential to mycobacterial growth and is not found in humans, therefore, it is a potential target for developing new anti-tuberculosis drugs |
4.2.1.50 | pyrazolylalanine synthase |
pharmacology |
production of beta-(pyrazol-1-yl)-L-alanine for pharmacological use by enzyme overexpressed in E. coli |
4.2.1.84 | nitrile hydratase |
pharmacology |
synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles |
4.2.2.1 | hyaluronate lyase |
pharmacology |
enzyme is a target for inhibitor design |
4.2.2.1 | hyaluronate lyase |
pharmacology |
enzyme can be used for production of pharmaceuticals as an alternative to bovine testicular hyaluronidase, BTH, because the production of BTH is stopped due to risk of BSE |
4.2.2.1 | hyaluronate lyase |
pharmacology |
enzyme is a target for development of antimicrobial agents |
4.2.2.1 | hyaluronate lyase |
pharmacology |
the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy |
4.2.2.1 | hyaluronate lyase |
pharmacology |
in vitro microbial hyaluronate lyase is able to split the hyaluronic acid in atherosclerotic plaques under release of calcium deposits and reduces in vivo the development of atherosclerotic lesions in hyperlipidaemic rabbits |
4.2.3.24 | amorpha-4,11-diene synthase |
pharmacology |
amorpha-4,11-diene is a precursor of artemisinin, an important agent in the treatment of malaria, produced via oxidation |
4.2.99.18 | DNA-(apurinic or apyrimidinic site) lyase |
pharmacology |
the enzyme is a potential target in cancer treatment |
4.3.1.18 | D-Serine ammonia-lyase |
pharmacology |
the D-serine dehydratase gene is an excellent marker, especially in the construction of strains for which the use of antibiotic resistance genes as selective markers is not allowed |
4.3.1.18 | D-Serine ammonia-lyase |
pharmacology |
decrease in D-serine content may provide a therapeutic strategy for the treatment of the neurological disorders in which overstimulation of N-methyl-D-aspartate receptors plays a pathological role. D-Serine dehydratase (Dsd1p), which acts dominantly on D-serine, may be a useful D-serine reducing agent. A linear 5-kDa polyethylene glycol (PEG) is conjugated to Dsd1p and the effects of PEG-conjugation on its biochemical and pharmacokinetic properties are examined. PEG-Dsd1p retains activity, specificity, and stability of the enzyme. The PEG modification extended the serum half-life of Dsd1p in mice 6fold, from 3.8 h to 22.4 h. PEG-Dsd1p is much less immunogenic compared to the unmodified enzyme. Intraperitoneal administration of PEG-Dsd1p is effective in decreasing the D-serine content in the mouse hippocampus |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
the ability of PAL to catalyze the conversion of L-Phe into nontoxic compounds in the absence of additional cofactors leads to its use as a therapeutic agent for the treatment of phenylketonuria |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
enzyme substitution therapy for the treatment of phenylketonuria |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
enzyme substitution therapy with the phenylalanine ammonia lyase is a new approach to the treatment of patients with phenylketonuria |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
the enzyme is specifically advantageous for the production of the hypertension drug 2-chloro-L-phenylalanine |
4.3.1.24 | phenylalanine ammonia-lyase |
pharmacology |
the shift of the pH-optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme, the prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria |
4.3.1.25 | phenylalanine/tyrosine ammonia-lyase |
pharmacology |
enzyme substitution therapy for the treatment of phenylketonuria |
4.3.1.25 | phenylalanine/tyrosine ammonia-lyase |
pharmacology |
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients |
4.3.2.1 | argininosuccinate lyase |
pharmacology |
argininosuccinate lyase (ASL) is overexpressed in breast cancer and downregulation of argininosuccinate lyase decreases tumor growth by inhibiting cyclin A2 and NO. Administration of ASL shRNA may be a treatment to prevent cancer cell proliferation and induce cancer cell death |
4.3.2.10 | imidazole glycerol-phosphate synthase |
pharmacology |
development of allosteric antibiotics, herbicides, and antifungal compounds because the enzyme is absent in mammals but provides an entry point to fundamental biosynthetic pathways in plants, fungi, and bacteria |
4.3.2.10 | imidazole glycerol-phosphate synthase |
pharmacology |
the enzyme is a potential therapeutic target absent in mammals but present in bacteria, plants, and fungi. Many plant and human pathogens that infect the immunocompromised patient have an IGPS that is highly homologous to the Saccharomyces cerevisiae and Thermotoga maritima enzymes |
4.3.3.2 | strictosidine synthase |
pharmacology |
cooverexpression of geraniol-10-hydroxylase and strictosidine synthase improves anti-cancer drug camptothecin accumulation in Ophiorrhiza pumila |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
enzyme structure analysis for design of novel therapeutics against bacterial pathogen |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
enzyme structure guides design of novel therapeutics |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
structure of the enzyme guides the design of novel therapeutics against the methicillin-resistant pathogen |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
the enzyme is a promising antibiotic target |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
the enzyme is a target for antibiotics |
4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
pharmacology |
the enzyme is an anti-cholera target |
4.4.1.4 | alliin lyase |
pharmacology |
allicin contributes to the prevention of stroke and arteriosclerosis. An acid resistant capsule is filled with pellets of alliin and alliinase. In the intestine, alliin and alliinase are dissolved and alicin is liberated |
4.4.1.4 | alliin lyase |
pharmacology |
a triggered antimicrobial system based on different sulfoxide substrates and alliinase might be superior to the application of conventional fungicides or allicin itself |
4.6.1.1 | adenylate cyclase |
pharmacology |
activation of cardiac adenylyl cyclase isozyme ACVI expression increases the function of the failing ischemic heart in mice, overview. Increased left ventricular ACVI content also markedly reduces mortality and increases left ventricular function after acute myocardial infarction in mice |
4.6.1.1 | adenylate cyclase |
pharmacology |
pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme |
4.6.1.2 | guanylate cyclase |
pharmacology |
activators of sGC may be beneficial in the treatment of a range of diseases including systemic and pulmonary hypertension, heart failure, atherosclerosis, peripheral arterial occlusive disease, thrombosis and renal fibrosis, overview |
4.6.1.2 | guanylate cyclase |
pharmacology |
alternative splicing can regulate endogenous ANP/GC-A signaling, thus, angiotensin II-induced alternative splicing of GC-A may represent a mechanism for reducing the sensitivity to atrial natriuretic peptide |
4.6.1.2 | guanylate cyclase |
pharmacology |
sGC is a target for therapeutic intervention in pulmonary arterial hypertension |
4.6.1.2 | guanylate cyclase |
pharmacology |
pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme |
4.6.1.18 | pancreatic ribonuclease |
pharmacology |
radical-scavenging effects of the ribonuclease inhibitor CPRI may contribute to its function in the cell protection from peroxidative injuries unrelated to inhibition of RNases |
4.6.1.18 | pancreatic ribonuclease |
pharmacology |
inhibitors can be the starting point for the development of compounds that can be used as pharmaceuticals against pathologies associated with ribonuclease A homologues such as human angiogenin, which is implicated in tumor induced neovascularization |