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