EC Number   |
Recommended Name |
Application |
|---|
    3.5.1.1 | asparaginase |
medicine |
the enzyme is widely used in chemotherapy for treatment of children with acute lymphoblastic leukemia, in vivo and in vitro resistance of the cells to the enzyme can occur |
| 3.5.1.1 | asparaginase |
medicine |
asparaginase is used in the treatment of acute lymphoblastic leukemia. It depletes plasma asparagine and glutamine, killing leukemic lymphoblasts but also causing immunosuppression. Asparaginase reduces maturing populations of normal B and T cells in thymus, bone marrow, and spleen of mice. Oral consumption of alanyl-glutamine mitigates metabolic stress in spleen, supporting the peripheral immune system and cell-mediated immunity during asparaginase chemotherapy |
| 3.5.1.1 | asparaginase |
medicine |
L-asparaginase is an anticancer agent. Developing an asparaginase production process based on bran of Glycine max as a substrate in solid state fermentation is economically attractive as it is a cheap and readily available raw material in agriculture-based countries |
| 3.5.1.1 | asparaginase |
medicine |
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy |
| 3.5.1.1 | asparaginase |
medicine |
the enzyme is important to the treatment of acute lymphoblastic leukemia. Intravenous PEG-asparaginase (L-asparaginase covalently linked to polyethylene glycol) will eliminate painful injection, and achieve rapid peak levels and asparagine depletion |
| 3.5.1.1 | asparaginase |
medicine |
chemotherapeutic agent |
| 3.5.1.1 | asparaginase |
medicine |
treatment of lymphoma |
| 3.5.1.1 | asparaginase |
medicine |
asparaginase is one of the important bioactive compounds, which have curative effects in cancer treatment |
| 3.5.1.1 | asparaginase |
medicine |
L-asparaginase II from Erwinia carotovora may represent an important alternative therapy in the treatment of acute childhood lymphoblastic leukaemia, despite its promising lower glutaminase activity than Escherichia coli and Erwinia chrysanthemi L-asparaginases II |
| 3.5.1.1 | asparaginase |
medicine |
the enzyme is an important biopharmaceutical product used in the treatment of acute lymphoblastic leukaemia |
| 3.5.1.1 | asparaginase |
medicine |
anticancer drug |
| 3.5.1.1 | asparaginase |
medicine |
the enzyme is an important drug in the treatment of childhood acute lymphoblastic leukemia |
| 3.5.1.1 | asparaginase |
medicine |
the recombinant enzyme potentiate a lectin's induction of leukemic K562 cell apoptosis |
| 3.5.1.1 | asparaginase |
medicine |
enzyme potentiates a lectin's induction of leukemic K562 cell apoptosis, allowing lowering of the drug dosage and shortening of the incubation time |
| 3.5.1.1 | asparaginase |
medicine |
covalent immobilization of enzyme on functionalized aluminium oxide nanoparticles (AONP) and titanium oxide nanoparticles (TONP) for anticancer therapy. The nano-bioconjugates are optimally active at pH 7.0 and 40°C. TONP-asparaginase activity is enhanced in the presence of NH4+ (160%) and Mn2+ (165%) while AONP-asparaginase bioconjugates show increased relative activity with ethyl acetate (142%) and toluene (160%). The nano-bioconjugates display good reusability and maintain over 90% average activity after nine successive cycles. Maximum cytotoxicity (61%) is noticed with AONP-asparaginase against human leukemia MOLT-4 cells. AONP-asparaginase shows better affinity to L-asparagine as compared to free enzyme |
| 3.5.1.1 | asparaginase |
medicine |
enzyme shows antitumor proterties with IC50 values 0.036 mg/ml for MCF-7 cells, 0.037 mM/ml for HCT-116 cells, 0.046 mg/ml for Hep-G2 cells, respectively |
| 3.5.1.1 | asparaginase |
medicine |
L-asparaginase may significantly alter the interactions between microvascular endothelial cells, colon cancer cells, and components, resulting in colon cancer cell injury |
| 3.5.1.1 | asparaginase |
medicine |
purified L-asparaginase does not show hemolysis effect on blood erythrocytes. Recombinant L-asparaginase retains 50% of its initial activity after 90 and 60 min incubation in serum and trypsin separately |
| 3.5.1.1 | asparaginase |
medicine |
recombinant enzyme is able to inhibit the proliferation of K-562 and Jurkat cell lines |
| 3.5.1.1 | asparaginase |
medicine |
the anticancer activity of purified asparaginase is comparable or higher than that of commercial Escherichia coli asparaginase. The purified enzyme induces apoptotic cell death in dose-dependent manner, probybly via activation of anintrinsic apoptotic pathway. The purified enzyme is nontoxic for human noncancerous FR-2 cells and human blood lymphocytes |
| 3.5.1.1 | asparaginase |
medicine |
the purified enzyme inhibits the growth of human cell lines Hep-G2, MCF-7 and PC-3 with IC50 values of 14 microg/ml, 12.5 microg/ml and 37 microg/ml, respectively |
| 3.5.1.1 | asparaginase |
medicine |
the purified enzyme shows cytotoxicity for the MOLT-4 leukemic cell lineage |
| 3.5.1.2 | glutaminase |
medicine |
enzyme therapy at the dose of 10 unit/mouse in ascites tumor bearing mice, elicits a reduction in tumor growth. At day 5, 10 and 15 it is reduced by 60%, 95% and 89% respectively. The life span of the enzyme treated mice increases significantly with respect to control mice |
| 3.5.1.2 | glutaminase |
medicine |
depresses some pro-inflammatory factors that occur during prolonged, exhaustive exercise |
| 3.5.1.2 | glutaminase |
medicine |
acivicin along with Escherichia coli glutaminase synergistically reduces in vitro proliferation and matrigel invasion of human MCF-7 and OAW-42 cells. Combination of acivicin with glutaminase may provide a better therapeutic option than either of them separately for treating human breast and ovarian cancer |
| 3.5.1.2 | glutaminase |
medicine |
purified L-glutaminase has a high toxic effect on Hela and Hep G2 cell lines with an IC50 value 18 and 12 microg/ml, respectively, and a moderate cytotoxic effect on HCT-116 and MCF7 cells, with an IC50 value 44 and 58 microg/ml, respectively |
| 3.5.1.2 | glutaminase |
medicine |
strategy to overcome acquired erlotinib resistance in NSCLC by inhibiting glutaminase activity. Compound 968, an inhibitor of the glutaminase C, when combined with erlotinib potently inhibits the cell proliferation of erlotinib-resistant NSCLC cells HCC827ER and NCI-H1975. The combination of compound 968 and erlotinib decreases glutaminase C and EGFR protein expression and inhibits glutaminase C activity in HCC827ER cells. Compound 968 combined with erlotinib down-regulates the glutamine and glycolysis metabolism in erlotinib-resistant cells |
| 3.5.1.3 | omega-amidase |
medicine |
in patients with liver disease and encephalopathy there is a good correlation between degree of neurological dysfunction and increase in alpha-ketoglutaramate in cerebrospinal fluid, omega-amidase is suitable for determination of alpha-ketoglutaramate |
| 3.5.1.4 | amidase |
medicine |
therapy |
| 3.5.1.4 | amidase |
medicine |
down-regulated state of FAAH - through its effects on CB1 and opioid receptor in the brain reward circuitry - promotes ethanol drinking behavior. Manipulation of the FAAH activity might represent a novel therapeutic target for the treatment of ethanol dependence |
| 3.5.1.4 | amidase |
medicine |
FAAH inhibition shows potential utility for the clinical treatment of persistent and neuropathic pain |
| 3.5.1.5 | urease |
medicine |
enhancement of intragastric enzyme activity is not strictly a function of pH-value, but is related to differential effects of the availability of nickel, which is required for enzyme activity |
| 3.5.1.5 | urease |
medicine |
lack of enzyme activity in most enterohaemorrhagic strains is due to a premature stop codon in ureD encoding a chaperone protein of the urease gene cluster |
| 3.5.1.5 | urease |
medicine |
use of jack bean urease as a model enzyme for Helicobacter pylori urease. Development of organobismuth components without antifungal activity against Saccharomyces cerevisiae but with antibacterial activity |
| 3.5.1.5 | urease |
medicine |
the action of urease in the upper intestinal tract is exploited in a non-invasive urease breath test for the diagnosis of bacterial infections of Helicobacter pylori: 13C- or 14C-labelled urea is ingested, and if the bacterium is present in the stomach, the urea is converted into isotope-labelled carbon dioxide. This is absorbed into the blood and exhaled in the breath, where it is detected by mass spectrometer or scintillation counter |
| 3.5.1.5 | urease |
medicine |
a novel immunoconjugate (L-DOS47) is developed and characterized as a therapeutic agent for tumors expressing CEACAM6. The single domain antibody AFAIKL2, which targets CEACAM6, is expressed in the Escherichia coli BL21 (DE3) pT7-7 system. High purity urease is extracted and purified from Jack bean meal. AFAIKL2 is activated using N-succinimidyl [4-iodoacetyl]aminobenzoate (SIAB) as the cross-linker and then conjugated to urease. The specificity and cytotoxicity of L-DOS47 is confirmed by screening in four cell lines (BxPC-3, A549, MCF7, and CEACAM6-transfected H23). BxPC-3, a CEACAM6-expressing cell line is most susceptible to L-DOS47. L-DOS47 is a potential therapeutic agent in human phase I clinical studies for nonsmall cell lung cancer |
| 3.5.1.5 | urease |
medicine |
importance of overall cryptococcal urease inhibition, rather than of its enzymatic activity alone, for the future development of therapeutic tools targeting cryptococcosis |
| 3.5.1.5 | urease |
medicine |
site targeted delivery of urease along with chemotherapeutic drugs can be a promising tool for anti-cancer applications. Urease shows its inhibitory effects on cancer cell lines through the generation of toxic ammonia, which in turn increases the pH of the surrounding medium. This increase in extracellular pH, enhances the cytotoxic effect of weak base chemotherapeutic drugs, doxorubicin (0.05 mM) and vinblastine (0.100 mM) in the presence of urease (5 U/ml) and urea (0-4 mM) significantly |
| 3.5.1.6 | beta-ureidopropionase |
medicine |
mutation analysis in patients with cloned genes |
| 3.5.1.6 | beta-ureidopropionase |
medicine |
analysis of putative enzyme defects in patients with neurological disfunctions |
| 3.5.1.6 | beta-ureidopropionase |
medicine |
pharmacogenetic studies in patients receiving fluoropyrimidine-based chemotherapy should include genetic variants in dihydropyrimidinase (DPYS) and beta-ureidopropionase (UPB1), in addition to DPYD, to improve the understanding of their contribution to severe toxicity from fluoropyrimidine-based chemotherapy. Potential unknown underlying causal variants linked to the associated dihydropyrimidinase and beta-ureidopropionase variants may have a clinically relevant effect on fluoropyrimidine toxicity and should be investigated |
| 3.5.1.12 | biotinidase |
medicine |
plasma biotinidase activity assay for diagnosis and screen newborn infants for biotinidase deficiency, treatment of inborn metabolism errors with large doses of biotin |
| 3.5.1.12 | biotinidase |
medicine |
naturally occuring missense mutations result in biotinidase deficiency, an autosomal recessively inherited disorder in which affected individuals have multiple carboxylase deficiency due to secondary deficiency of free biotin |
| 3.5.1.12 | biotinidase |
medicine |
thirteen novel mutations in children with biotinidase deficiency. Biotinidase deficiency is a defect in the recycling of the vitamin biotin. Biotin supplementation can markedly improve the neurological and cutaneous symptoms of affected children and prevents symptoms in children identified by newborn screening or treated since birth |
| 3.5.1.12 | biotinidase |
medicine |
serum biotinidase is a sensitive and specific biochemical marker of hepatic dysfunction |
| 3.5.1.14 | N-acyl-aliphatic-L-amino acid amidohydrolase |
medicine |
N-acetyl-L-cysteine used for drugs against lung disorders and HIV infections, test of potential antitumor agents |
| 3.5.1.14 | N-acyl-aliphatic-L-amino acid amidohydrolase |
medicine |
preparation of commercially important amino acids as components for semisynthetic penicillins and cephalosporins |
| 3.5.1.14 | N-acyl-aliphatic-L-amino acid amidohydrolase |
medicine |
the enzyme is an important biomarker with potential prognostic utility in patients with delayed graft function following renal transplantation |
| 3.5.1.15 | aspartoacylase |
medicine |
diagnosis of Canavan disease, an autosomal recessive neurodegenerative disorder characterized by aspartoacylase deficiency, technique for prenatal diagnosis |
| 3.5.1.15 | aspartoacylase |
medicine |
mutations in the aspartoacylase aspA gene are implicated as the cause of Canavan Disease |
| 3.5.1.16 | acetylornithine deacetylase |
medicine |
enzymatic target for a novel set of antibiotics |
| 3.5.1.18 | succinyl-diaminopimelate desuccinylase |
medicine |
inhibition of the catalytic action of the microbial enzyme DapE is fatal to the growth of bacteria and critical to the use of this enzyme as a potential antibiotic target |
| 3.5.1.19 | nicotinamidase |
medicine |
Riemerella anatipestifer AS87_01735 gene encodes PncA, which is an important virulence factor. The Yb2DELTApncA mutant can be used as a novel live vaccine candidate |
| 3.5.1.19 | nicotinamidase |
medicine |
the absence of nicotinamidase in humans makes it a promising drug target |
| 3.5.1.20 | citrullinase |
medicine |
clinical biochemistry, therapeutic measurement of citrulline |
| 3.5.1.23 | ceramidase |
medicine |
CDase from Pseudomonas aeruginosa may be a virulence factor in infections, may be involved in the ceramide deficiency in the horny layer of the epidermis of patients with atopic dermatitis suffering from bacterial infections |
| 3.5.1.23 | ceramidase |
medicine |
patients with the lipid storage disorder, the Farber disease, have a marked AC deficiency |
| 3.5.1.23 | ceramidase |
medicine |
Farber disease is diagnosed by the demonstration of reduced acid ceramidase activity, abnormally high ceramide levels in cultured cells, biopsy samples or urine, and the presence of Farber bodies, comma-shaped curvilinear tubular structures. The enzyme is likely to continue to be a target for new drug development in cancer and other disorders |
| 3.5.1.23 | ceramidase |
medicine |
downregulation of acid ceramidase increases sensitivity to radiation |
| 3.5.1.23 | ceramidase |
medicine |
in human prostate tissues, acid ceramidase and cathepsin B overexpression are strongly associated and may relate to poor outcome |
| 3.5.1.23 | ceramidase |
medicine |
inhibition of acid ceramidase is useful in cancer treatment |
| 3.5.1.23 | ceramidase |
medicine |
because of its central role in the ceramide metabolism, the enzyme may offer a novel molecular target in disorders with dysfunctional ceramide-mediated signaling |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
protein encapsulation is an excellent tool to protect enzymes during transit through gastric conditions and release enzyme activity in the proximal small intestine |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
using bile salt deconjugation to lower serum cholesterol levels in hypercholesteremic patients and prevent hypercholesteremia in normal people is of great interest |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
effect of oral administration to Wistar rats of the immobilized bile salt hydrolase enzyme on serum cholesterol, triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia, overview |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
active BSH derived from the probiotic Lactobacillus johnsonii strain La1 may yield anti-giardial effects in vitro and in vivo. The enzyme may be useful in approaches for the treatment of widely spread but neglected infectious disease, such as giardiasis, both in human and in veterinary medicine |
| 3.5.1.24 | choloylglycine hydrolase |
medicine |
bile salt hydrolase (BSH) active probiotic strains are being used in the treatment of hypercholesterolemia related diseases |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
fluorometric assay in blood samples allows specific detection of the enzyme defect in aspartylglycosaminuria patients |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
diagnosis of aspartylglycosaminuria in urine samples |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
deficient AGA activity results in a lysosomal storage disease, aspartylglucosaminuria, resulting in progressive neurodegeneration, most of disease-causing mutations lead to defective molecular maturation of AGA |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
enzyme deficiency or its absence gives rise to aspartylglycosaminuria, an autosomal recessive inherited disorder that results in the accumulation of glycoasparagines in lysosomes, most common disorder of glycoprotein metabolism |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
enzyme deficiency or its absence gives rise to aspartylglycosaminuria, the most common disorder of glycoprotein metabolism |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
a high dose enzyme replacement therapy with glycosylasparaginase in newborn aspartylglycosaminuria mice is up to 2fold more effective in reducing the amount of the accumulated storage material from the brain tissue than enzyme replacement therapy in adult aspartylglycosaminuria animals |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
human glycosylasparaginase is a potential anticancer agent to induce apoptosis in L-asparagine-dependent cancer cells |
| 3.5.1.26 | N4-(beta-N-acetylglucosaminyl)-L-asparaginase |
medicine |
use of codon-optimized AGA may be beneficial for the therapy options in treatment of the lysosomal storage disorder aspartylglucosaminuria (AGU) |
| 3.5.1.33 | N-acetylglucosamine deacetylase |
medicine |
nonfunctional enzyme mutant, reduced virulence in intraperitoneal mouse model |
| 3.5.1.38 | glutamin-(asparagin-)ase |
medicine |
L-glutaminase has a significant efficiency against Hep-G2 cell (IC50 6.8x02g/ml) and HeLa cells (IC50 8.3 g/ml), while the growth of MCF-7 cells is not affected. L-glutaminase has a moderate cytotoxic effect against HCT-116 cells (IC50 64.7 g/ml) and RAW 264.7 cells (IC50 59.3 g/ml). In vivo, L-glutaminase shows no observed changes in liver, kidney functions, hematological parameters and slight effect on red blood cells and level of platelets after 10 days of rabbit's injection |
| 3.5.1.41 | chitin deacetylase |
medicine |
chitosan is necessary for cell wall integrity in Cryptococcus neoformans. Chitin deacetylases and the chitosan made by them may prove to be excellent antifungal targets |
| 3.5.1.60 | N-(long-chain-acyl)ethanolamine deacylase |
medicine |
modulation of the tissue levels of palmitoylethanolamide by inhibition of enzymes responsible for the breakdown of this lipid mediator, including the N-acylethanolamine acid amidase, may represent therefore a therapeutic strategy for the treatment of pain and inflammation |
| 3.5.1.88 | peptide deformylase |
medicine |
attractive target for antibacterial drug discovery |
| 3.5.1.88 | peptide deformylase |
medicine |
the enzyme is a potential antibacterial and antimalarial drug target |
| 3.5.1.88 | peptide deformylase |
medicine |
possible target for new broad spectrum antimicrobial agents |
| 3.5.1.88 | peptide deformylase |
medicine |
antibacterial activity against clinically significant Gram-positive and Gram-negative pathogens |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase has been considered an attractive target for antibacterial chemotherapy |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase has been considered as a potential target in antimicrobial chemotherapy |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase inhibitors have a strong potential to be used as antibiotics |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase is a promising antibacterial and herbicide target |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase is a target for novel antibiotics |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase may be a potential target for designing new antibiotics |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase represents a target for the discovery of broad spectrum antibacterial drugs |
| 3.5.1.88 | peptide deformylase |
medicine |
potential drug target, antimalarial drugs |
| 3.5.1.88 | peptide deformylase |
medicine |
target for anti-Helicobacter pylori drugs |
| 3.5.1.88 | peptide deformylase |
medicine |
target for antibacterial agents |
| 3.5.1.88 | peptide deformylase |
medicine |
target for antibacterial agents against Staphylococcus aureus |
| 3.5.1.88 | peptide deformylase |
medicine |
target for the development of new antibacterial drugs |
| 3.5.1.88 | peptide deformylase |
medicine |
target of antibiotic drugs |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase becomes a target for the design of new antibiotics |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase is a target for the design of novel antibiotics |
| 3.5.1.88 | peptide deformylase |
medicine |
peptide deformylase is a target protein for the development of anti-bacterial drugs |
