EC Number |
Recommended Name |
Application |
---|
3.5.1.88 | peptide deformylase |
drug development |
human peptide deformylase (HsPDF) is an important target for anticancer drug discovery |
3.5.1.88 | peptide deformylase |
drug development |
peptide deformylase (PDF) is considered an excellent target to develop antibiotics |
3.5.1.88 | peptide deformylase |
drug development |
peptide deformylase (PDF), a metalloprotease, is an important antibacterial drug target |
3.5.1.88 | peptide deformylase |
drug development |
the enzyme HsPDF is a cancer therapeutic target |
3.5.1.88 | peptide deformylase |
drug development |
the enzyme is a drug target for antibacterial agents. Classification of PDF inhibitors, overview |
3.5.1.88 | peptide deformylase |
drug development |
the enzyme is a drug target in malaria treatment |
3.5.1.88 | peptide deformylase |
drug development |
the enzyme is an important antibacterial drug target |
3.5.1.88 | peptide deformylase |
drug development |
the enzyme is an important target to develop antibacterial agents |
3.5.1.89 | N-acetylglucosaminylphosphatidylinositol deacetylase |
drug development |
the enzyme is a target in the treatment of African sleeping sickness |
3.5.1.92 | pantetheine hydrolase |
drug development |
the highly sensitive fluorescent assay for the hydrolysis of pantothenate-7-amido-4-methylcoumarin as substrate to pantothenic acid and 7-amino-4-methylcoumarin could be a powerful tool for target validation and drug lead identification and characterization |
3.5.1.97 | acyl-homoserine-lactone acylase |
drug development |
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection) |
3.5.1.98 | histone deacetylase |
drug development |
the enzyme might be a promising target for the development of novel anti-babesial drugs |
3.5.1.99 | fatty acid amide hydrolase |
drug development |
FAAH is an attractive target for treating pain |
3.5.1.103 | N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase |
drug development |
enzyme MshB is a target for the discovery of drugs to treat tuberculosis |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
enzyme is an attractive target against Pseudomonas infection |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
lipid A is an essential component of the outer membranes of most Gram-negative bacteria, making LpxC an attractive target for antibiotic design |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
LpxC is a target for the development of antimicrobial agents in the treatment of Gram negative infections |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
LpxC represents a highly attractive target for a novel antibacterial drug |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
target for development of anti-infective drugs against gram-negative bacteria |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
the enzyme is a promising target for antibacterial drug development, structure-guided drug discovery of broad spectrum Gram-negative antibiotics |
3.5.1.108 | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
drug development |
the enzyme is a target for antibiotic therapy and structure-based drug design |
3.5.1.119 | Pup amidohydrolase |
drug development |
the Pup-proteasome enzymes are essential for full virulence and persistence in the mammalian host. As such, the Pup-proteasome enzymes are potential targets for development of antituberculosis therapeutics. Such development requires sensitive and robust assays for measurements of enzymatic activities and the effect of examined inhibitors. An in vitro activity assay for Dop, the first enzyme in the Pup-proteasome system is described, that is ased on fluorescence anisotropy measurements. This assay is simple, sensitive, and compatible with a high-throughput format for screening purposes and can be reliably and conveniently used for detailed kinetic measurements of Dop activity |
3.5.1.124 | protein deglycase |
drug development |
secreted DJ-1 levels in serum and DJ-1-binding compounds will be a diagnostic biomarker and therapeutic drug for neurodegenerative diseases |
3.5.2.B2 | (+)-gamma-lactamase |
drug development |
application of the enzyme in antiviral drug synthesis. The enzyme catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir |
3.5.2.B2 | (+)-gamma-lactamase |
drug development |
the enzyme can be a promising candidate of biocatalyst for industrial applications of highly valuable chiral pharmaceutical chemicals |
3.5.2.B2 | (+)-gamma-lactamase |
drug development |
the enzyme is an ideal catalyst for the preparation of carbocyclic nucleosides of pharmaceutical interest. IT can be used in a scalable bioprocess and is an efficient, economical, and environmentally route for producing optically pure (-)-gamma-lactam |
3.5.2.B2 | (+)-gamma-lactamase |
drug development |
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir |
3.5.2.3 | dihydroorotase |
drug development |
the essential enzyme is a target for antibacterial drug design |
3.5.2.3 | dihydroorotase |
drug development |
the substantial difference between bacterial and mammalian DHOs makes the bacterial enzyme a promising drug target for disrupting bacterial growth and thus an important candidate to evaluate as a response to antimicrobial resistance on a molecular level |
3.5.2.6 | beta-lactamase |
drug development |
the enzyme is a target for treatment of Mycobacterium abscessus infections |
3.5.2.6 | beta-lactamase |
drug development |
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2 |
3.5.2.6 | beta-lactamase |
drug development |
enzyme BlaC is a rational enzyme target for therapeutic agents in treatment of tuberculosis caused by Mycobacterium tuberculosis |
3.5.2.6 | beta-lactamase |
drug development |
the PWP triad is an evolutionarily conserved motif unique to class A beta-lactamases aligning its allosteric site and hence is an effective potential target for enzyme regulation and selective drug design |
3.5.3.1 | arginase |
drug development |
the application of rhArg-PEG alone or in combination with existing chemotherapeutic drugs may represent a specific and effective therapeutic strategy against human hepatocellular carcinoma |
3.5.3.1 | arginase |
drug development |
arginase catalyzes the first committed step in the biosynthesis of polyamines that enable cell growth and hence potential drug target for the treatment of leishmaniasis |
3.5.3.6 | arginine deiminase |
drug development |
ADI is a potential anti-tumor drug for the treatment of argine-auxotrophic tumors, e.g. hepatocellular carcinoma and melanoma |
3.5.3.6 | arginine deiminase |
drug development |
anti-tumor drug |
3.5.3.6 | arginine deiminase |
drug development |
arginine deiminase is a therapeutic protein for cancer therapy of arginine-auxotrophic tumors. An ammonia detection-based screening system for arginine deiminase activity improvement at low arginine concentrations is developed and validated by identifying variants of the Pseudomonas plecoglossicida arginine deiminase with improved activity at physiological arginine concentrations. Four amino acid substitutions are identified to reduce S0.5 values or increase kcat values. The antiproliferation activity of the improved enzyme variant K30R/C37R/L148P/V291L is investigated and compared to wild-type and mutant enzyme K5T/D38H/D44E/A128T/E296K/H404R by in vitro experiments with two relevant melanoma cell lines under physiological conditions. Pseudomonas plecoglossicida arginine deiminase variant K30R/C37R/L148P/V291L is a highly attractive candidate to be used as therapeutic protein for the treatment of arginine-auxotrophic melanomas |
3.5.3.6 | arginine deiminase |
drug development |
L-arginine deiminase has a powerful anticancer activity against various tumors, via arginine depletion, arresting the cell cycle at G1 phase. The free and PEGylated enzyme exhibits a similar cytotoxic efficacy against HCT, HEP-G2, and MCF7 cells, lower than the cytotoxic efficacy of to enzyme covalently immobilized on dextran. The in vitro anticancer activity of the enzyme against HCT, MCF7, and HEPG-2 cells is increased by five-, three-, and threefold upon covalent modification by dextran |
3.5.3.6 | arginine deiminase |
drug development |
possibility of a use of the enzyme as a potential anticancer drug. Purified enzyme exhibits profound antiproliferative activity against Hep-G2 cells. Purified enzyme induces apoptosis in the Hep-G2 cells by DNA fragmentation |
3.5.3.6 | arginine deiminase |
drug development |
the enzyme is a particularly attractive therapeutic target for breast cancer because it is recruited by the estrogen receptor to endoplasmic reticulum target gene promoters where it citrullinates histone H3 at R26, leading to ER-target gene activation |
3.5.3.6 | arginine deiminase |
drug development |
the enzyme shows potential anticancer activity against various arginine-auxotrophic tumors. The higher antigenicity, structural instability and in vivo proteolysis are the major challenges that limit this enzyme from further clinical implementation. The anticancer activity of the enzyme to breast (MCF-7), liver (HepG-2) and colon (HCT8, HT29, DLD1 and LS174 T) cancer cell lines is increased by 1.7folds with dextran conjugation in vitro. Pharmacokinetically, the half-life time of ADI is increased by 1.7folds upon dextran conjugation, in vivo. From the biochemical and hematological parameters, arginine deiminase has no signs of toxicity to the experimental animals |
3.5.3.6 | arginine deiminase |
drug development |
the lack of this enzyme in the human host makes arginine deiminase an attractive target for drug design against Giardia intestinalis |
3.5.3.12 | agmatine deiminase |
drug development |
Campylobacter jejuni agmatine deiminase is a potentially important target for combatting antibiotic resistance |
3.5.3.15 | protein-arginine deiminase |
drug development |
PAD4 is a leading target for the development of a rheumatoid arthritis pharmaceutical |
3.5.3.15 | protein-arginine deiminase |
drug development |
the enzyme is a particularly attractive therapeutic target for breast cancer because it is recruited by the estrogen receptor to endoplasmic reticulum target gene promoters where it citrullinates histone H3 at R26, leading to ER-target gene activation |
3.5.4.3 | guanine deaminase |
drug development |
because these enzymes play an important role in nucleotide metabolism, they are relevant targets in anticancer and antibacterial therapies |
3.5.4.4 | adenosine deaminase |
drug development |
enzyme inhibitor FR234938 might be effective as an anti-rheumatic and anti-inflammatory drug by modulating the host-defense concentrations of adenosine |
3.5.4.4 | adenosine deaminase |
drug development |
adenosine deaminase inhibitors have potential as anti-inflammatory drugs or immunosuppressants |
3.5.4.4 | adenosine deaminase |
drug development |
because these enzyme plays an important role in nucleotide metabolism, they are relevant targets in anticancer and antibacterial therapies |
3.5.4.4 | adenosine deaminase |
drug development |
Plasmodium parasites lack enzymes critical for de novo purine synthesis and thus rely on purine salvage to supply precursors for nucleic acid synthesis and energy metabolism. Thus, the purine salvage pathway is an attractive drug target |
3.5.4.4 | adenosine deaminase |
drug development |
progesterone treatment may prevent epileptic activity by decreasing adenosine deaminase levels |
3.5.4.5 | cytidine deaminase |
drug development |
CDA is a target for development of specific enzyme inhibitors with potential anti-proliferative activity on cell growth of Mycobacterium tuberculosis, the major causative agent of tuberculosis |
3.5.4.9 | methenyltetrahydrofolate cyclohydrolase |
drug development |
the bifunctional enzyme is a target for design of parasite-specific inhibitors as structure-based drugs |
3.5.4.10 | IMP cyclohydrolase |
drug development |
the enzyme is a potential target for antineoplastic intervention, design of IMPCH inhibitors, overview |
3.5.4.10 | IMP cyclohydrolase |
drug development |
the enzyme is an important drug target |
3.5.4.19 | phosphoribosyl-AMP cyclohydrolase |
drug development |
the enzyme is identified as drug target. Brucella melitensis is a pathogenic gram-negative bacterium which is known for causing zoonotic diseases (Brucellosis). The organism is highly contagious and is used as bioterrorism agent against humans |
3.5.4.37 | double-stranded RNA adenine deaminase |
drug development |
ADAR1 is a potential therapeutic target in a subset of cancers |
3.5.4.37 | double-stranded RNA adenine deaminase |
drug development |
the enzyme (ADAR1) promotes the Zika virus replication by inhibiting the activation of protein kinase PKR. The enzyme can be a potential target of antiviral drugs |
3.6.1.5 | apyrase |
drug development |
Ecto-NTPDase1 is a target candidate in chemotherapy of Chagas disease |
3.6.1.5 | apyrase |
drug development |
the NTPDase isozymes are targets for development of potent and selective drug-like NTPDase inhibitors |
3.6.1.9 | nucleotide diphosphatase |
drug development |
NPP1 has been proposed as a drug target for the treatment of glioblastoma |
3.6.1.12 | dCTP diphosphatase |
drug development |
the enzyme is a drug target |
3.6.1.12 | dCTP diphosphatase |
drug development |
DCTPP1 counteracts the cytotoxic effect of the antitumoral demethylating agent decitabine (5-aza-deoxycytidine) by removing 5-aza-dCTP from the nucleotide pool and is being studied as a potential drug target to improve decitabine-based chemotherapy |
3.6.1.12 | dCTP diphosphatase |
drug development |
the enzyme is a factor involved in the mode of action of decitabine with potential value as enzymatic targets to improve decitabine-based chemotherapy |
3.6.1.23 | dUTP diphosphatase |
drug development |
dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors |
3.6.1.23 | dUTP diphosphatase |
drug development |
induced fit drug design |
3.6.1.23 | dUTP diphosphatase |
drug development |
inhibitor development against the enzyme can be useful in antiviral and anticancer therapy |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a potential antiparasitic drug target |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme might be a target for drug development |
3.6.1.23 | dUTP diphosphatase |
drug development |
dUTPase is a promising antituberculotic drug target |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a target for development of antimicrobial agents |
3.6.1.23 | dUTP diphosphatase |
drug development |
the nuclear isoform of the enzyme is a target for anticancer chemotherapeutic strategies |
3.6.1.23 | dUTP diphosphatase |
drug development |
dUTPase family of enzymes are promising targets for anticancer and antimicrobial therapies |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a potential drug target against malaria |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a target for anti-malarial drugs |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a target for development of therapeutic drugs against EBV infection |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a target for drugs against campylobacteriosis |
3.6.1.23 | dUTP diphosphatase |
drug development |
the enzyme is a factors involved in the mode of action of decitabine with potential value as enzymatic targets to improve decitabine-based chemotherapy |
3.6.1.31 | phosphoribosyl-ATP diphosphatase |
drug development |
because of its essentiality for growth in vitro, HisE is a potential drug target for tuberculosis |
3.6.4.10 | non-chaperonin molecular chaperone ATPase |
drug development |
Hsp70 proteins are targets for the drug-based treatments for cancers, misfolding diseases, and protein folding disorders |
3.6.4.10 | non-chaperonin molecular chaperone ATPase |
drug development |
human heat shock protein 90 is a target in cancer drug discovery, inhibition of ATP hydrolysis is a validated avenue for the development of anticancer therapies |
3.6.4.10 | non-chaperonin molecular chaperone ATPase |
drug development |
reconstitution of the entire Plasmodium translocon of exported proteins, PTEX, to aid structure-based design of anti-malarial drugs |
3.6.4.B10 | chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing) |
drug development |
development of cell-based CCT inhibitors using peptide reagents and HSF1A, a benzyl-pyrazole-based small molecule |
3.6.4.B10 | chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing) |
drug development |
development of small-molecule inhibitors of TRiC as potential antiviral therapeutics |
3.6.4.B10 | chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing) |
drug development |
the enzyme is a target for the specific treatments of AML1-ETO-positive leukemia. AML1-ETO suppression by small interfering RNAs (siRNAs) supports normal myeloid differentiation of t(8,21)-positive leukemic cells which highlights AML1-ETO as a major clinical target to treat AML. Inhibition of HSP70/90, two major proteostasis regulators, has shown antileukemic effects in AML1-ETO positive cells. Moreover, the mammalian cytosolic chaperonin TRiC (or CCT) modulates the synthesis, folding and activity of AML1-ETO by direct association, primarily through its DNA-binding domain (AML1-175), and that HSP70 promotes this interaction |
3.6.4.13 | RNA helicase |
drug development |
the enzyme is a target for anti-HCV drug development |
3.6.4.13 | RNA helicase |
drug development |
the enzyme is a target for development of specific antiviral inhibitors |
3.6.4.13 | RNA helicase |
drug development |
the multifunctional NS3 protein from Dengue virus is a target for the design of antiviral inhibitors |
3.6.4.13 | RNA helicase |
drug development |
enzyme p68 is a drug target in the treatment of cancer, e.g. breast cancer |
3.6.5.1 | heterotrimeric G-protein GTPase |
drug development |
mutants of transducin represent a major tool in designing potential therapeutical strategies for a group of visual diseases |
3.6.5.2 | small monomeric GTPase |
drug development |
the enzyme Der may be an ideal cellular target against which antibiotics can be developed, lead compounds inhibiting Der GTPase provide scaffolds for the development of antibiotics against antibiotic-resistant pathogenic bacteria |
3.7.1.3 | kynureninase |
drug development |
the enzym eis a target for the design of potent and/or selective inhibitors of bacterial kynureninase |
3.7.1.3 | kynureninase |
drug development |
the enzyme is a target for the design of potent and/or selective inhibitors of human kynureninase |
3.10.1.1 | N-sulfoglucosamine sulfohydrolase |
drug development |
the enzyme is a target for the development of structure-based drug design for the devastating neurodegenerative disorder mucopolysaccharidosis type IIIA or Sanfilippo A syndrome |
3.13.2.1 | adenosylhomocysteinase |
drug development |
because of the prominent role of SAM-dependent transmethylation in capped methylated structure production at the 5'-terminus of viral mRNA, SAHH inhibitors could be developed to be broad-spectrum antiviral agents |
4.1.1.11 | aspartate 1-decarboxylase |
drug development |
the enzyme is a target for structure-based drug development |
4.1.1.11 | aspartate 1-decarboxylase |
drug development |
the enzyme is a good drug target |
4.1.1.11 | aspartate 1-decarboxylase |
drug development |
the PanDZ complex is a target for antibiotic development |
4.1.1.17 | ornithine decarboxylase |
drug development |
the enzyme ODC is a drug target in human malignancies, such as skin cancer |