EC Number   |
Recommended Name |
Application |
|---|
   3.1.13.1 | exoribonuclease II |
analysis |
- |
| 3.1.25.1 | deoxyribonuclease (pyrimidine dimer) |
analysis |
- |
| 3.1.26.1 | Physarum polycephalum ribonuclease |
analysis |
- |
| 3.1.30.1 | Aspergillus nuclease S1 |
analysis |
- |
 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
analysis |
- |
| 3.2.1.68 | isoamylase |
analysis |
- |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
analysis |
- |
| 4.6.1.21 | Enterobacter ribonuclease |
analysis |
- |
| 4.1.1.39 | ribulose-bisphosphate carboxylase |
analysis |
1 pg of plant mRNA, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, is used to determine the efficiency of RT-PCR in general, and as a external reference gene for normalization of gene expression |
| 3.1.4.37 | 2',3'-cyclic-nucleotide 3'-phosphodiesterase |
analysis |
2',3'-cyclic nucleotide 3'-phosphodiesterase is a stable marker for in situ detection of canine but not rat olfactory ensheathing cells |
| 1.14.13.24 | 3-hydroxybenzoate 6-monooxygenase |
analysis |
3-hydroxybenzoate 6-hydroxylase (3HB6H, EC 1.14.13.24) from Rhodococcus jostii RHA1 is used as a lipid-containing reference protein for enzyme 4-hydroxybenzoate 1-hydroxylase, 4HB1H (EC 1.14.13.64). Models for Cp_4HB1H from Candida parapsilosis strain CBS604, Fo_4HB1H-like from Fusarium oxysporum, and VibMO1 from Boreostereum vibrans (UniProt ID A0A167KUL3) are generated using Rhodococcus jostii Rj_3HB6H (PDB ID 4bk1) and Pseudomonas putida Pp_SALH (PDB ID 5evy) as template structures, overview |
| 6.3.4.10 | biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase |
analysis |
96-well plate assay for high-throughput analysis of holocarboxylase synthetase activity by biotinylation of the polypeptide p67, which comprises the 67 C-terminal amino acids in human propionyl-CoA carboxylase, including the biotin-binding site lysine-669, using IRDye-streptavidin and infrared spectroscopy. The minimal concentration of recombinant HCS that can be detected by this assay is less than 1.08 nmol/l. Jurkat cells contain 0.14 U of HCS activity [in micromol of biotinylated p67 formed/(nmol/l HCS h)] in 400 microg of total protein |
| 1.6.2.4 | NADPH-hemoprotein reductase |
analysis |
96-well plate format assay to follow cytochrome c reduction |
| 1.14.13.2 | 4-hydroxybenzoate 3-monooxygenase |
analysis |
a bienzyme-based Clark electrode is developed for the interference-free determination of L-glutamate. This sensor is based on the specific dehydrogenation by L-glutamate dehydrogenase (EC 1.4.1.3) in combination with p-hydroxybenzoate hydroxylase (EC 1.14.13.2). The enzymes are entrapped by a poly(carbamoyl) sulfonate hydrogel on a Teflon membrane |
| 3.5.4.4 | adenosine deaminase |
analysis |
a capillary electrophoresis method for simultaneous analysis of adenosine deaminase in red blood cells is developed. The method is also successfully applied in the inhibitor screening from traditional Chinese medicines |
| 1.14.15.3 | alkane 1-monooxygenase |
analysis |
a certain type of alkB gene is present in almost everymember of the genus Rhodococcus. The alkB gene type may be applicable for differentiating closely related Rhodococcus species, properly assigning environmental isolates to existing Rhodococcus species, and assessing whether a new Rhodococcus isolate represents a novel species of the genus |
| 1.7.3.3 | factor-independent urate hydroxylase |
analysis |
a colorimetric 96-well microtiter plate assay for the determination of urate oxidase activity and its kinetic parameters based on hydrogen peroxide quantitation. The general advantages of the colorimetric assay are easy handling of large amounts of samples at the same time, the possibility of automation, and the need for less material |
| 3.1.11.2 | exodeoxyribonuclease III |
analysis |
a combined treatment of nucleosomes with micrococcal nuclease and exonuclease III overcomes micrococcal nuclease sequence preference and produces nucleosomal DNA trimmed symmetrically and precisely at the core/linker junctions regardless of the underlying DNA sequence. Combined micrococcal nuclease/exonuclease III digestion can be applied to in situ chromatin for unbiased genome-wide mapping of nucleosome positions that is not ifluenced by DNA sequences at the core/linker junctions. The same approach can be also used for the precise mapping of the extent of linker DNA protection by H1 and other protein factors associated with nucleosome linkers |
| 2.7.11.24 | mitogen-activated protein kinase |
analysis |
a concept and implementation of a new simple inhibitor screening method applicable for a broad range of human proteins by using transformed bacteria is reported |
| 4.2.1.42 | galactarate dehydratase |
analysis |
a continuous assay for L-talarate/galactarate dehydratase is develped using circular dichroism. The advantages that this assay method offers are that initial rate measurements may be obtained much more rapidly than is possible using fixed-time assays (e.g., semicarbazide derivatization or NMR methods) and it is much less complex than a coupled assay, which is often limited by the availability and specific properties of the coupling enzymes |
| 2.1.1.11 | magnesium protoporphyrin IX methyltransferase |
analysis |
a continuous enzyme-coupled spectrophotometric assay for ChlM from Synechocystis sp. PCC 6803 is reported |
| 4.2.1.42 | galactarate dehydratase |
analysis |
a convenient, direct continuous circular dichroism-based assay is developed for following the L-talarate/galactarate dehydratase-catalyzed conversion of meso-galactarate to 5-dehydro-4-deoxy-D-glucarate. The advantages that this assay method offers are that initial rate measurements may be obtained much more rapidly than is possible using fixed-time assays (e.g., semicarbazide derivatization or NMR methods) and it is much less complex than a coupled assay, which is often limited by the availability and specific properties of the coupling enzymes |
| 6.2.1.7 | cholate-CoA ligase |
analysis |
a coupled assay for bile acid:CoA ligase and glycination of bile acid-CoA catalyzed by bile acid-CoA:glycine N-acetyltransferase |
| 5.4.2.7 | phosphopentomutase |
analysis |
a coupled optical enzyme assay |
| 1.1.3.13 | alcohol oxidase |
analysis |
a dual biosensor analysis system based on alcohol oxidase and alcohol dehydrogenase for the simultaneous analysis of methanolethanol mixtures is developed. The alcohol dehydrogenase biosensor quantifies only the ethanol in the range 0.3-8 mmol/l without interference from methanol in concentrations as high as 100 mmol/l. The alcohol oxidase biosensor is able to respond to both analytes in the range 3-70 mmol/l for methanol and 15110 mmol/l for ethanol. The concentration of ethanol and methanol from the sample is determined by processing analytical signals obtained from both biosensors |
| 1.14.16.4 | tryptophan 5-monooxygenase |
analysis |
a Dugesia japonica TPH antibody is a useful marker for serotonergic neurons in planarians |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
analysis |
a fast, robust, and sensitive spectrophotometric activity assay based on a peroxidase activity of LPMO, using 2,6-dimethoxyphenol and H2O2. The high molar absorption coefficient of the formed Product coerulignone displays a high molar absorption coefficinet that makes the assay sensitive and allows reliable activity measurements of LPMO in concentrations of approx. 0.5-50 mg/l |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
analysis |
a fast, robust, and sensitive spectrophotometric activity assay based on a peroxidase activity of LPMO, using 2,6-dimethoxyphenol and H2O2. The high molar absorption coefficient of the formed Product coerulignone displays a high molar absorption coefficinet that makes the assay sensitive and allows reliable activity measurements of LPMO in concentrations of approx. 0.550 mg/L |
| 3.5.2.20 | isatin hydrolase |
analysis |
a fluorescence-based enzymatic assay is developed that can quantify isatin, a putative stress biomarkerin blood samples. A phase extraction of isatin followed by a second phase extraction combined with an enzymatic reaction performed by an isatin hydrolase is used to extract and quantify isatin in whole blood samples |
| 1.13.12.24 | calcium-regulated photoprotein |
analysis |
a fusion protein composed of the synthetic IgG-binding domain (ZZ domain) derived from Staphylococcus aureus protein A and apoaequorin (apoAQ) is expressed in Escherichia coli periplasm. Incubation with coelenterazine gives ZZ-aequorin which can be used as a reporter for detecting IgG. The measurable range of IgG coated on a 96-well plate is 1-1000 ng/ml |
| 5.1.1.7 | diaminopimelate epimerase |
analysis |
a high-performance liquid chromatography method for the simultaneous assay of diaminopimelate epimerase and decarboxylase |
| 2.4.1.1 | glycogen phosphorylase |
analysis |
a highly sensitive and convenient assay for glycogen phosphorylase activity by analysing its chainlengthening action on a fluorogenic maltooligosaccharide derivative in a glucose-1-phosphate-rich medium. A maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase, and pyridylaminated maltohexaose is the most suitable substrate. Pyridylaminated maltoheptaose produced by the chain elongation reaction can be isolated and quantified at 10 fmol. Method has about 1000 times greater sensitivity than the spectrophotometric phosphate assay |
| 1.13.11.2 | catechol 2,3-dioxygenase |
analysis |
a highly sensitive microbial biosensor is constructed using the recombinant Escherichia coli BL21-C23O cell as bio-recognition element for catechol detection. Based on the synergistic effect of catechol 2,3-dioxygenase and nanoporous gold, the resulting microbial biosensor exhibits good performance for catechol detection with high sensitivity, strong anti-interference and good stability |
| 2.3.2.15 | glutathione gamma-glutamylcysteinyltransferase |
analysis |
a HPLC method for the analysis of the activity of phytochelatin synthase is developed |
| 4.3.1.2 | methylaspartate ammonia-lyase |
analysis |
a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
analysis |
a method for poly(3-hydroxybutyrate) (PHB) depolymerase activity determination. The method is based on online determination of NaOH consumption rates necessary to neutralize 3-hydroxybutyric acid and/or 3-hydroxybutyrate oligomers produced during the hydrolysis reaction and requires a pH-stat apparatus equipped with a softwarecontrolled microliter pump for rapid and accurate titration. The method is universally suitable for hydrolysis of any type of polyhydroxyalkanoate or other molecules with hydrolyzable ester bonds, allows the determination of hydrolysis rates of as low as 1 nmol/min, and has a dynamic capacity of at least 6 orders of magnitude |
| 2.7.1.78 | polynucleotide 5'-hydroxyl-kinase |
analysis |
a method for real-time monitoring of the activity and kinetics of T4 polynucleotide kinase by use of a singly fluorophore-labeled DNA-hairpin smart probe coupled with lambda exonuclease cleavage is described |
| 4.1.1.39 | ribulose-bisphosphate carboxylase |
analysis |
a method is established to remove ribulose bisphosphate carboxylase/oxygenase from plant samples to obtain high quality and high resolution 2D gels in proteome analysis |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
analysis |
a method to investigate quantitatively and qualitativly the hydrolysis of different types of poly(3-hydroxybutyrate) by selected PHB depolymerases. The method is based on the derivatization of 3-hydroxybutyrate oligomers into bromophenacyl derivates and separation by high performance liquid chromatography. The method allows the separation and quantification of 3-hydroxyutyrate and 3-hydroxybutyrate oligomers up to the octamer |
| 2.3.2.3 | lysyltransferase |
analysis |
a method to obtain a stable enriched membrane fraction containing MprF, and the techniques necessary to quantitatively monitor its activity in vitro and in vivo is reported |
| 1.14.14.3 | bacterial luciferase |
analysis |
a minimized cascade for Lux with greater ease of use, utilizes a chemoenzymatic reaction with biomimetic nicotinamide 1-benzyl-1,4-dihydronicotinamide in place of the flavin reductase reaction in the Lux system. The minimized cascade reaction can be applied to monitor bioluminescenceof the Lux reporter in eukaryotic cells effectively, and can achieve higher efficiencies than the system with flavin reductase |
| 2.8.2.1 | aryl sulfotransferase |
analysis |
a modified variant of sulfotransferase assay employs permeabilized fission yeast cells (enzyme bags). A new and convenient SULT activity assay is based on the sulfation of a proluciferin compound, which is catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1 |
| 2.8.2.2 | alcohol sulfotransferase |
analysis |
a modified variant of sulfotransferase assay employs permeabilized fission yeast cells (enzyme bags). A new and convenient SULT activity assay is based on the sulfation of a proluciferin compound, which is catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1 |
| 2.8.2.4 | estrone sulfotransferase |
analysis |
a modified variant of sulfotransferase assay employs permeabilized fission yeast cells (enzyme bags). A new and convenient SULT activity assay is based on the sulfation of a proluciferin compound, which is catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1 |
| 1.5.1.17 | alanopine dehydrogenase |
analysis |
a nonfluorescent negative stain to visualize the alanopine dehydrogenase isoenzyme pattern in crude-tissue homogenates from very small worms |
| 3.1.11.3 | exodeoxyribonuclease (lambda-induced) |
analysis |
a novel method for real-time monitoring of the activity and kinetics of T4 polynucleotide kinase (PNK) by use of a singly fluorophore-labeled DNA-hairpin smart probe (SP) coupled with lambda exonuclease (lambda exo) cleavage. |
| 2.3.2.6 | lysine/arginine leucyltransferase |
analysis |
a novel method to quantify L/F transferase activity by matrix assisted laser desorption/ionization time-of-flight mass spectrometry, MALDI-TOF, is reported |
| 1.1.3.9 | galactose oxidase |
analysis |
a photoelectrochemical biosensor for quantitative detection of galactose is obtained immobilizing galactose oxidase on TiO2 nanorod arrays modified F-doped tin oxide (FTO) electrode. The direct electron transfer to galactose oxidase is achieved. The generated photocurrent of the stable platform is significantly enhanced after the addition of galactose in solution and the photocurrent intensity shows linear relationship with the galactose concentration. CaCl2, uric acid and ascorbic acid have no interference with the detection of galactose. The sensor can be reused and applied to measure the concentration of galactose in lactose-free milk |
| 4.3.1.3 | histidine ammonia-lyase |
analysis |
a potentiometric sensor is made by immobilizing histidine ammonia-lyase on an ammonia gas-sensing electrode |
| 6.5.1.1 | DNA ligase (ATP) |
analysis |
a procedure for fast, sensitive and quantitative measurement of DNA ligase activity in crude cell extract |
| 3.5.1.52 | peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase |
analysis |
a procedure to map N-glycosylation sites is presented, it can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup |
| 2.2.1.1 | transketolase |
analysis |
a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins like transketolase |
| 4.1.99.14 | spore photoproduct lyase |
analysis |
a rapid separation technique for detecting and quantitating SP by chromatography : tritiated thymine-containing photoproducts from trifluoroacetic acid-hydrolyzed DNA purified from UV-irradiated cells or spores of Bacillus subtilis are identified and isolated from paper chromatograms, subjected to HPLC on a Microsorb phenyl 5-micrometer column using 100% water as the mobile phase, and detected by scintillation counting of collected fractions |
| 2.4.1.212 | hyaluronan synthase |
analysis |
a rapid, continuous, and convenient three-enzyme coupled UV absorption assay is developed to quantitate the glucuronic acid and N-acetylglucosamine transferase activities of hyaluronan synthase. Activity is measured by coupling the UDP produced from the PmHAS-catalyzed transfer of UDP-GlcNAc and UDP-GlcUA to a hyaluronic acid tetrasaccharide primer with the oxidation of NADH. Using a fluorescently labeled primer, the products are characterized by gel electrophoresis. The assay can be used to determine kinetic parameters, inhibition constants, and mechanistic aspects of this enzyme. In addition, it can be used to quantify PmHAS during purification of the enzyme from culture media |
| 6.3.5.4 | asparagine synthase (glutamine-hydrolysing) |
analysis |
a rapid, inexpensive micro assay that can be adapted for large numbers of samples |
| 2.7.7.72 | CCA tRNA nucleotidyltransferase |
analysis |
a relatively short segment of the coding region for tRNA nucleotidyltransferase has a higher discriminatory potential than most established diagnostic DNA markers. The selected gene region of the tRNA nucleotidyltransferase reveals a seven- to 30fold higher distinction potential between closely related Vibrio or Aspergillus species, respectively. Even in the presence of a 1000fold excess of human genomic DNA, no unspecific amplicons are produced |
| 1.2.1.3 | aldehyde dehydrogenase (NAD+) |
analysis |
a reliable, enzyme-coupled assay for measuring glycerol dehydratase activity in crude-cell extract is developed using 1,2-propanediol as the substrate. In the assay, 1,2-propanediol is converted to propionaldehyde, which is quickly converted to 1-propionic acid by aldehyde dehydrogenase (with the production of NADH) or to 1-propanol by yeast alcohol dehydrogenase (with the consumption of NADH). The change in NADH concentration, as monitored at 340 nm spectrophotometrically, manifested as a straight line for 3 min, from which the glycerol dehydratase activity can be determined. Cells are assumed to have been disintegrated by physical methods (Bead Beater or French Press), not by chemical methods. The assay method should prove to be applicable to recombinant strains developed for the production of 3-hydroxypropionic acid and/or and/or 1,3-propanediol from glycerol |
| 4.1.1.39 | ribulose-bisphosphate carboxylase |
analysis |
a sensitive and robust mixed-mode high performance liquid chromatography-tandem mass spectrometry method is developed for the qualitative and quantitative determination of sugar phosphates |
| 1.13.12.9 | phenylalanine 2-monooxygenase |
analysis |
a simple and rapid enzymic determination of L-Phe with L-phenylalanine oxidase (deaminating and decarboxylating) |
| 5.1.99.1 | methylmalonyl-CoA epimerase |
analysis |
a simple direct assay for DL-methylmalonyl-coenzyme A racemase which is based on the fact that the proton on C-2 of methylmalonyl-CoA is replaced by a proton in the medium during racemization |
| 6.3.2.12 | dihydrofolate synthase |
analysis |
a simple radioassay for dihydrofolate synthetase activity and its application to an inhibition study of new pteroate analogs |
| 5.3.3.7 | aconitate DELTA-isomerase |
analysis |
a simple sensitive and specific method for measuring aconitate isomerase in plants, which depends on the release of tritium from labeled trans-aconitate |
| 3.2.1.166 | heparanase |
analysis |
a simple, accurate, and robust biochemical assay for heparanase activity that uses a commercially available homogeneous substrate (fondaparinux) with a single enzymatic cleavage point and, thus, does not have the problems associated with using heparan sulfate-based assays. The assay is suitable for testing heparanase inhibitors and could easily be adapted for use in high-throughput screening applications |
| 4.3.1.15 | Diaminopropionate ammonia-lyase |
analysis |
a specific enzymatic procedure for the determination of neurotoxic components, derivatives of L-2,3-diaminopropanoate with diaminopropanonate ammonia-lyase |
| 5.4.2.6 | beta-Phosphoglucomutase |
analysis |
a specific method for the quantitative determination of beta-glucose 1-phosphate |
| 4.4.1.36 | hercynylcysteine S-oxide lyase |
analysis |
a synthetic route toward ergothioneine pathway intermediates for the preparation of stable isotopically labelled hercynine-d3, which is enzymatically converted to ergothioneine-d3 |
| 3.4.99.B2 | D-aspartyl endopeptidase |
analysis |
a system for screening D-Asp-containing proteins is developed by using D-aspartyl endopeptidase and a two-dimensional gel electrophoresis |
| 3.4.13.20 | beta-Ala-His dipeptidase |
analysis |
a validated method for measuring serum carnosinase activity in serum and heparin plasma |
| 2.3.3.10 | hydroxymethylglutaryl-CoA synthase |
analysis |
a visible wavelength spectrophotometric assay suitable for high-throughput screening of 3-hydroxy-3-methylglutaryl-CoA synthase is established |
| 2.1.1.364 | [histone H3]-lysine4 N-methyltransferase |
analysis |
ab initio quantum mechanical/molecular mechanical molecular dynamics simulations with the umbrella sampling method to determine free energy profiles for histone lysine methylation catalyzed by SET7/9 and its corresponding uncatalyzed reaction in aqueous solution, activation free energy barrier for the methyl transfer reaction catalyzed by SET7/9 is 22.5 kcal/mol, which agrees with the experimental value of 20.9 kcal/mol very well, SET7/9 lowers the barrier for the methyl-transfer reaction step by 8.4 kcal/mol compared with the uncatalyzed reaction |
| 2.1.1.63 | methylated-DNA-[protein]-cysteine S-methyltransferase |
analysis |
ability to specifically label AGT fusion proteins in the presence of endogenous AGT, after brief incubation of the cells with a small-molecule inhibitor, may significantly broaden the scope of application of AGT fusion proteins for studying protein function in living cells |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
accurate, simple and sensitive method for the quantitative analysis of triglycerides. Assay for triglycerides using glycerol dehydrogenase and a water-soluble formazan dye, WST-8 |
| 3.4.17.23 | angiotensin-converting enzyme 2 |
analysis |
ACE2-based biosensor designed to detect both SARS-CoV-2 S1 mutations and neutralizing antibodies. In binding mode, the biosensor works by detecting binding of the spike protein to an immobilized ACE2 receptor and is able to detect S1 proteins of the alpha (500 pg/ml) and beta variants (10 ng/ml), as well as wild-type S1 (10 ng/ml), of SARSCoV-2 and it distinguishes wild-type SARS-CoV-2 S1 from the S1 alpha and beta variants via color differences. A modification to the protocol enables the ACE2-based biosensor to operate in blocking mode to detect neutralizing antibodies in serum samples from COVID-19 patients |
| 2.5.1.18 | glutathione transferase |
analysis |
acetylcholinesterase and glutathione S-transferase activities in Daphnia magna are used in the standardized Daphnia magna immobility toxicity test for toxic substances e.g. in water quality monitoring, overview |
| 2.4.1.B64 | glucosyltransferase Waag |
analysis |
activity assay for WaaG using 14C-labeled UDP-glucose and lipopolysaccharide purified from a WaaG deletion strain of Escherichia coli. Addition of the lipids phosphatidylglycerol and cardiolipin, as well as the detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate increase activity |
| 1.11.1.9 | glutathione peroxidase |
analysis |
activity is important in predicting tissue redox state |
| 3.11.1.2 | phosphonoacetate hydrolase |
analysis |
activity stain for detection of carbon-phosphorus cleavage by phosphonoacetate hydrolase in PAGE gels |
| 2.7.7.38 | 3-deoxy-manno-octulosonate cytidylyltransferase |
analysis |
adaptation of a simple colorimetric assay for diphosphate to the enzyme 3-deoxy-D-manno-octulosonate cytidylyltransferase. This assay can be combined with the malachite green assay for phosphate to form an assay system capable of determining phosphate and diphosphate in the same solution. The assay system has the potential for simultaneous screening of the 3-deoxy-D-manno-octulosonate biosynthesis pathway |
| 3.2.2.9 | adenosylhomocysteine nucleosidase |
analysis |
adaptation of an enzyme-coupled colorimetric assay based on the quantification of homocysteine produced from S-adenosyl-L-homocysteine in presence of enzyme and S-ribosylhomocysteinase to cyclopropane fatty acid synthase for high-throughput screening of compound libraries |
| 3.5.3.15 | protein-arginine deiminase |
analysis |
adding bicarbonate to commercial peptidyl arginine deiminase activity kits could increase assay performance and biological relevance |
| 1.1.5.5 | alcohol dehydrogenase (quinone) |
analysis |
adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinonealcohol dehydrogenase could be a marker to analyse both growth and oxidation ability in some acetic acid bacteria, especially those of the genus Acetobacter |
| 1.3.3.4 | protoporphyrinogen oxidase |
analysis |
advantages of the continuous spectrofluorimetric assay over the discontinuous assay is of importance for both the kinetic characterization of recombinant PPOs and the detection of low concentrations of this enzyme in biological samples |
| 1.3.3.4 | protoporphyrinogen oxidase |
analysis |
advantages of the continuous spectrofluorimetric assay over the discontinuous assay is of importance for both the kinetic characterization of recombinant PPOs and the detection of low concentrations of this enzyme in biological samples, may be useful for assessing diminished PPO activities in variegate porphyria patient samples |
| 3.4.21.5 | thrombin |
analysis |
affinity probe capillary electrophoresis/laser-induced fluorescence polarization assay for detection of human thrombin using a specific aptamer as probe. Monovalent and bivalent cations promoting the formation of a stable G quadruplex conformation in the aptamer may enhance the binding of the aptamer and thrombin, while cations like K+ and Mg2+ cannot stabilize the affinity complex. Without the use of typical cations, a highly sensitive assay of human thrombin was developed with the corresponding detection limits of 4.38×10?19 and 2.94×10?19 mol in mass for standard solution and human serum, respectively |
| 2.1.3.3 | ornithine carbamoyltransferase |
analysis |
after administration of carbon tetrachloride, allyl alcohol, D-galactosamine, lipopolysaccharide, and concanavalin A, the significant increase in the serum levels of the markers is faster in type-I arginase and ornithine carbamoyltransferase than aspartate aminotransferase and alanine aminotransferase. The extent of the increase at the peak is always higher in type-I arginase and ornithine carbamoyltransferase than in spartate aminotransferase and alanine aminotransferase |
| 2.4.1.17 | glucuronosyltransferase |
analysis |
after infection of Sf9 insect cells with increasing amounts of recombinant baculovirus, encoding either UGT1A9 or UGT2B7, the correlation between glucuronidation rates and degree of infection follows different trends, depending on whether activity is the actual activity measured or is corrected for UDP-glucuronosyltransferase expression level. Above a certain low level of infection, further increases in infection ratios lead to a large decline in normalized activity, presumably due to the presence of full-length but inactive enzyme in the sample. Inaccuracies in comparison of normalized activity between different batches of a recombinant UDP-glucuronosyltransferase can be reduced by lowering the degree of infection of the insect cells, in combination with careful monitoring of UDP-glucuronosyltransferase expression. Poly-His-containing peptides, fused to the UDP-glucuronosyltransferase C-terminus, allow sensitive immunodetection of expressed enzymes with monoclonal antibodies. A minor increase in the Km values has been detected in the His-tagged UDP-glucuronosyltransferases, but no changes in parameters such as the kinetic model and the effects of albumin addition |
| 1.4.1.1 | alanine dehydrogenase |
analysis |
alanine dehydrogenase from Streptomyces anulatus can be used as a bioreceptor in an ammonium biosensor that can detect ammonium ions in water samples. The sensor shows linear response in the range of 0.1-300mM NH4+ with the detection limit of 0.01 mM NH4+ and response time of 20 s. The sensor is showing good response at wide pH range (pH 5-11) and temperature range (20-50°C) suggesting its usage at ambient and non-ambient conditions. The sensor is successfully validated with Nessler's reagent method by using different water samples |
| 1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
analysis |
ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy |
| 1.1.1.58 | tagaturonate reductase |
analysis |
aldonate estimation |
| 3.1.3.1 | alkaline phosphatase |
analysis |
ALP and fat storage are tightly linked during preadipocyte maturation. Measurement of ALP activity may be a sensitive and rapid technique for the quantification of intracellular lipid accumulation |
| 6.1.1.21 | histidine-tRNA ligase |
analysis |
alternating catalysis requires a mechanism for coupling events between active sites, presumably through conformational changes propagated between these active sites, a version of HisRS is developed that features the site-specific incorporation of extrinsic environmentally sensitive fluorescent probes, allowing the adenylation reaction to be followed by stopped-flow fluorometry |
| 3.4.13.22 | D-Ala-D-Ala dipeptidase |
analysis |
although catalytically ineffecient, the VanX substrate D-leucine-p-nitroanilide is an alternative substrate for VanX because it can be monitored directly and assayed spectrophotometrically which facilitates the routine analysis of enzyme catalysis and the screening discovery of potential VanX inhibitors. In addition, it is with leucine in its D form that possible activities from other contaminated species (other than VanX) in Escherichia coli JM109 are greatly reduced. Moreover, D-leucine-p-nitroanilide needs essentially no sophisticated synthetic chemistry for preparation |
| 4.4.1.20 | leukotriene-C4 synthase |
analysis |
although structural differences near the active site and along the C-terminal alpha-helix V suggest that the mouse and human enzymes may function differently in vivo, the mouse enzyme is a useful tool in pharmacological research and drug development |
| 1.1.99.13 | glucoside 3-dehydrogenase (acceptor) |
analysis |
amperometic enzyme electrode for sugar detection |
| 1.4.1.15 | lysine dehydrogenase |
analysis |
amperometric biosensor for L-lysine based on immobilized enzyme |
| 1.5.1.36 | flavin reductase (NADH) |
analysis |
amperometric NADH biosensor system that employs the allosterically modulated reductase component of the 4-hydroxyphenylacetate hydroxylase in an adapted osmium(III)-complex-modified redox polymer film for analyte quantification. The activity of the reductase is enhanced upon binding of effector 4-hydroxy-phenylacetic acid, allowing the acceleration of the substrate conversion rate on the sensor surface by in situ addition or preincubation with 4-hydroxy-phenylacetic acid. Acceleration of NADH oxidation amplifies the response of the biosensor, with a 1.5fold increase in the sensitivity of analyte detection |
| 1.3.3.6 | acyl-CoA oxidase |
analysis |
amperometric propionate sensor |
| 2.8.3.1 | propionate CoA-transferase |
analysis |
amperometric propionate sensor |
| 1.1.3.13 | alcohol oxidase |
analysis |
amperometric sensor for ethanol based on one-step electropolymerization of thionine-carbon nanofiber nanocomposite containing alcohol oxidase. The ethanol biosensor can monitor ethanol ranging from 0.002 to 0.252 mM with a detection limit of 0.0017 mM. It displays a rapid response, an expanded linear response range as well as excellent reproducibility and stability |
| 4.2.1.46 | dTDP-glucose 4,6-dehydratase |
analysis |
an absorbance-based microtiter plate assay is developed for RmlB activity. It can be used for high-throughput screening of RmlB inhibitors |
