EC Number   |
Recommended Name |
Application |
|---|
    1.1.3.13 | alcohol oxidase |
analysis |
the enzyme is useful for construction of ethanol biosensors |
| 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 |
| 1.1.3.13 | 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 |
| 1.1.3.13 | alcohol oxidase |
analysis |
an amperometric biosensor for ethanol monitoring is developed and optimised. The biosensor uses poly(neutral red), as redox mediator, which is electropolymerised on carbon film electrodes and alcohol oxidase from Hansenula polymorpha as recognition element, immobilised by cross-linking with glutaraldehyde in the presence of bovine serum albumin as carrier protein. The biosensor is used for the determination of ethanol in Portuguese red and white wines. No significant interferences were found from compounds usually present in wine |
| 1.1.3.13 | alcohol oxidase |
analysis |
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts |
| 1.1.3.13 | alcohol oxidase |
analysis |
selection procedure for isolation of the mutant forms of AOX, and their use as a suitable bioelement for biosensor technologies. The created biosensor based on mAOX (from the strain CA2) was characterised by a decreased affinity towards analyzed substrates and slightly increased Vmax. The operational stability of the mAOX-immobilised electrode is not affected and remains similar to an electrode based on the natural enzyme. The described methodology opens up the possibility for construction of biosensors appropriate for precise, rapid, and cheap analysis of target analytes, e.g. ethanol in real samples of wines, beers or fermentation cultures |
| 1.1.3.13 | alcohol oxidase |
analysis |
the enzyme is useful in alcohol biosensor applications |
| 1.1.3.13 | alcohol oxidase |
analysis |
fabrication of a self-powered ethanol biosensor comprising a beta-NAD+-dependent alcohol dehydrogenase bioanode and a bienzymatic alcohol oxidase and horseradish peroxidase biocathode. beta-NAD+ is regenerated by means of a toluidine blue modified redox polymer. The biofuel cell exhibits an open-circuit voltage of approximately 660 mV and can be used as self-powered device for the determination of the ethanol content in liquor |
| 1.1.3.13 | alcohol oxidase |
analysis |
the behaviour of commercially available AOx and ADH enzymes is studied in 12 different biosensor designs towards butanol-1 detection in liquid media. Four out of twelve proposed designs demonstrate a good signal reproducibility and linear response (up to 14.6 mM of butanol) under very low applied potentials (from -0.02 to -0.32 V) |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
analysis |
development of a lactate biosensor through immobilization of lactate oxidase in an albumin and mucin composed hydrogel by gluitaraldehyde cross-linking and trapping between two polycarbonate membranes. Hydrogen peroxide produced is detected on a platinum electrode. The response time of the sensor to 0.010 mM lactate requires 90 s to give a 100% steady-state response of 0.079 microA. Linear behavior is obtained between0.7 microM and 1.5 mM. The detection limit calculated from the signal to noise ratio was 0.7 microM |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
analysis |
construction of a D-Lactate electrochemical biosensor. The electrode for detection of D-lactate is prepared by immobilizing dye-linked D-LDH and multi-walled carbon nanotube within Nafion membrane. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days |
| 1.1.3.17 | choline oxidase |
analysis |
investigation of an acetylcholinesterase/choline oxidase-based amperometric biosensor as a liqid chromatography detector for acetylcholine determination in brain tissue |
| 1.1.3.17 | choline oxidase |
analysis |
two-enzyme sensor for determination of choline esters prepared by covalent co-immobilization of choline oxidase and butyrylcholinesterase |
| 1.1.3.17 | choline oxidase |
analysis |
the immobilized enzyme is used in amperometric biosensors for choline detection, method evaluation |
| 1.1.3.17 | choline oxidase |
analysis |
determination of lead ions by inhibition of choline oxidase enzyme using an amperometric choline biosensor. Choline oxidase is immobilized on a glassy carbon electrode modified with multiwalled carbon nanotubes through cross-linking with glutaraldehyde. In the presence of choline oxidase, choline is enzymatically oxidized into betaine at -0.3 V versus Ag/AgCl reference electrode, lead ion inhibition of enzyme activity causing a decrease in the choline oxidation current. Under the best conditions for measurement of the lowest concentrations of lead ions, the choline oxidase/multiwalled carbon nanotubes/glassy carbon electrode gives a linear response from 0.1 to 1.0 nM Pb2+ and a detection limit of 0.04 nM |
| 1.1.3.17 | choline oxidase |
analysis |
development of a metal composite material based on zirconium dioxide decorated gold nanoparticles (ZrO2 at AuNPs), copper (I) oxide at manganese (IV) oxide (Cu2O at MnO2) and immobilized choline oxidase (ChOx) onto a glassy carbon electrode (GCE) (ChOx/Cu2O at MnO2-ZrO2 at AuNPs/GCE) for enhancing the electro-catalytic property, sensitivity and stability of the amperometric choline biosensor. The ChOx/Cu2O at MnO2-ZrO2 at AuNPs/GCE displays a good electrocatalytic response to the oxidation of the byproduct H2O2 from the choline catalyzed reaction. The modified electrode also provides a wide linear range of choline concentration from 0.5 to 1000.0 microM with good sensitivity and low detection limit (0.3 microM). The apparent Michaelis-Menten constant is 0.08 mM with Imax of 0.67 microA. The choline biosensor presents high repeatability, good reproducibility, long time of use and good selectivity without interfering effects from possible electroactive species such as ascorbic acid, aspirin, amoxicillin, caffeine, dopamine, glucose, sucrose and uric acid |
| 1.1.3.17 | choline oxidase |
analysis |
facile and sensitive colorimetric biosensor based on DNAzyme-choline oxidase coupling used for the determination of choline. In this method, choline oxidase produces H2O2 and betaine in the presence of choline and oxygen, then, the DNAzyme converts colorless ABTS into green ABTS+ radicals. The linear range and the limit of detection of this biosensor are 0.1-25 microM and 22 nM. Choline measurement using this biosensor shows satisfactory selectivity and repeatability. Its recovery is 96.95-107.73% in biological samples |
| 1.1.3.21 | glycerol-3-phosphate oxidase |
analysis |
co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase on to aryl amine glass beads affixed on plastic strip for determination of triglycerides in serum |
| 1.1.3.21 | glycerol-3-phosphate oxidase |
analysis |
building of an improved amperometric triglyceride biosensor using lipase nanoparticles/glycerol kinase nanoparticles/glycerol 3-phosphate oxidase nanoparticles/pencil graphite electrode as the working electrode, Ag/AgCl as the standard electrode and Pt wirebas auxiliary electrode. The biosensor shows optimum response within 2.5 s at a pH 7.0 and temperature of 35°C. It measures current due to electrons generated at 0.1 V against Ag/AgCl, from H2O2, which is produced from triolein by coimmobilized enzyme nanoparticles. Analytical recovery of added triolein in serum is 98.01. The biosensor can be employed for determination of triglycerides in the serum of apparently healthy subject and persons suffering from hypertriglyceridemia |
| 1.1.3.29 | N-acylhexosamine oxidase |
analysis |
enzyme may by useful for measurement of N-acetyl-beta-D-glucosaminidase |
| 1.1.3.38 | vanillyl-alcohol oxidase |
analysis |
development of a screening assay for the substrate specificity of para-phenol oxidases based on the detection of hydrogen peroxide using the ferric-xylenol orange complex method |
| 1.1.3.43 | paromamine 6'-oxidase |
analysis |
development of a coupled enzyme assays including 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide and phenazine methosulfate, resulting in the production of 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide formazan which can be monitored at 570 nm |
| 1.1.3.44 | 6'''-hydroxyneomycin C oxidase |
analysis |
development of a coupled enzyme assays including 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide and phenazine methosulfate, resulting in the production of 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide formazan which can be monitored at 570 nm |
| 1.1.5.2 | glucose 1-dehydrogenase (PQQ, quinone) |
analysis |
application of mutant enzyme S231K as a glucose sensor constituent. The mutant has more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme and retains catalytic activity similar to the wild-type enzyme |
| 1.1.5.2 | glucose 1-dehydrogenase (PQQ, quinone) |
analysis |
apoenzyme is used as a biological test system for the detection of very low amounts of pyrroloquinoline quinone |
| 1.1.5.2 | glucose 1-dehydrogenase (PQQ, quinone) |
analysis |
enzyme is used as coupling enzyme for monitoring carbohydrate-transport reactions, the method is particularly suited for determining transport reactions that are not coupled to any form of metabolic energy such as uniport reactions, or for characterizing mutant proteins with a defective energy-coupling mechanism or system with high-affinity constants for sugars |
| 1.1.5.2 | glucose 1-dehydrogenase (PQQ, quinone) |
analysis |
because of its high turnover number, PQQ-GDH is proposed as an enzyme label for the development of sensitive electrochemical enzyme-amplified bioaffinity assays. It has, for example, been applied to the amperometric detection of DNA hybrids or sandwich DNA aptamers at the surface of a carbon electrode |
| 1.1.5.2 | glucose 1-dehydrogenase (PQQ, quinone) |
analysis |
its high stability at high temperature makes this enzyme potentially useful for applications in biosensors or biofuel cells |
| 1.1.5.5 | alcohol dehydrogenase (quinone) |
analysis |
construction and evaluation of an ethanol sensor based on the enzyme using direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode, overview |
| 1.1.5.5 | alcohol dehydrogenase (quinone) |
analysis |
the enzyme can be used in biosensors, method development, overview |
| 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 |
| 1.1.5.9 | glucose 1-dehydrogenase (FAD, quinone) |
analysis |
possible use of the enzyme as amperometric glucose biosensor |
| 1.1.5.9 | glucose 1-dehydrogenase (FAD, quinone) |
analysis |
the enzyme can be used as O2-independent biosensor for glucoe detection |
| 1.1.5.14 | fructose 5-dehydrogenase |
analysis |
the enzyme is a satisfactory reagent for microdetermination of D-fructose |
| 1.1.98.3 | decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase |
analysis |
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout |
| 1.1.99.4 | dehydrogluconate dehydrogenase |
analysis |
enzymic microdetermination of 2-keto-D-gluconate |
| 1.1.99.6 | D-lactate dehydrogenase (acceptor) |
analysis |
construction of a D-Lactate electrochemical biosensor. The electrode for detection of D-lactate is prepared by immobilizing dye-linked D-LDH and multi-walled carbon nanotube within Nafion membrane. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days |
| 1.1.99.6 | D-lactate dehydrogenase (acceptor) |
analysis |
D-lactate content is of great interest for food analysis. A D-lactate sensing system using a thermostable dye-linked D-lactate dehydrogenase (Dye-DLDH) is developed. The electrode for detection of D-lactate is prepared by immobilizing the thermostable Dye-DLDH and multi-walled carbon nanotube (MWCNT) within Nafion membrane. The electrocatalytic response of the electrode is clearly observed upon exposure to D-lactate. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days |
| 1.1.99.13 | glucoside 3-dehydrogenase (acceptor) |
analysis |
amperometic enzyme electrode for sugar detection |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
analysis |
enzyme is used in highly selective amperometric biosensors |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
analysis |
cellobiose dehydrogense - electrode system for electrochemical applications |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
analysis |
development of biosensors, electrochemistry |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
analysis |
the enzyme has applications in lactose determination in food and as biosensor |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
analysis |
the enzyme is used in lactose determination in food |
| 1.1.99.29 | pyranose dehydrogenase (acceptor) |
analysis |
pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars |
| 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 |
| 1.2.1.3 | aldehyde dehydrogenase (NAD+) |
analysis |
spectrophotometric assay for the sensitive measurement of the glycerol dehydratase activity with a sub-nanomolar limit of detection. The assay method employs aldehyde dehydrogenase as a reporter enzyme, so the readout of the glycerol dehydratase activity is recorded at 340 nm as an increase in UV absorbance which results from NADH generation accompanied by oxidation of 3-hydroxypropionaldehyde to 3-hydroxypropionic acid. The glycerol dehydratase assay is performed under the reaction conditions where the aldehyde dehydrogenase activity overwhelms the GDHt activity (i.e., 50fold higher activity of aldehyde dehydrogenase relative to glycerol dehydratase activity), affording sensitive detection of glycerol dehydratase with 360 pM limit of detection |
| 1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
analysis |
ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy |
| 1.2.1.12 | glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) |
analysis |
GAPDH is a multi-functional protein that is used as a control marker for basal function, it is known to undergo cysteine oxidation under different types of cellular stress |
| 1.2.1.46 | formaldehyde dehydrogenase |
analysis |
presence of enzyme can be used as a selectable marker in DNA-mediated transformations |
| 1.2.1.73 | sulfoacetaldehyde dehydrogenase |
analysis |
the enzyme is useful for determination of sulfoacetaldehyde concentrations |
| 1.2.1.104 | pyruvate dehydrogenase system |
analysis |
sensitive and rapid assay procedures for human mitochondrial the pyruvate dehydrogenase (PDH) complex, the 2-oxoglutarate dehydrogenase (OGDH) complex and their 5 component enzymes, for use with crude tissue extracts |
| 1.2.1.105 | 2-oxoglutarate dehydrogenase system |
analysis |
sensitive and rapid assay procedures for human mitochondrial the pyruvate dehydrogenase (PDH) complex, the 2-oxoglutarate dehydrogenase (OGDH) complex and their 5 component enzymes, for use with crude tissue extracts |
| 1.2.3.3 | pyruvate oxidase |
analysis |
rapid detection of phosphate using immobilized pyruvate oxidase |
| 1.2.3.3 | pyruvate oxidase |
analysis |
biosensor for inorganic phosphate |
| 1.2.3.3 | pyruvate oxidase |
analysis |
construction of an amperometric biosensor using nanoparticles of pyruvate oxidase, immobilized covalently onto pencil graphite electrode. The biosensor shows ideal working within 5 s under defined conditions of pH 6.0 and 30°C at an applied voltage of -0.1 V. Under standard assay conditions, a linear response is obtained between pyruvate concentration from 0.001 to 6000 microM and current. Lower detection limit is 0.58 microM, the biosensor can be used for over 210 days for the measurement of pyruvate in blood sera |
| 1.2.3.3 | pyruvate oxidase |
analysis |
use of nanoparticles of commercially available pyruvate oxidase covalently immobilized onto gold electrode as amperometric pyruvate biosensor for detection of pyruvate in serum. The biosensor shows optimum response within 7.5 s, at a potential of 0.28 V, pH 5.5 and 35°C and a lower detection limit of 0.67 microM. The analytical recovery of added pyruvate in sera is 99.0% and 99.5% within and between batches. The biosensor can be utilized for detection of total pyruvate level in sera of apparently healthy individuals and patients suffering from cardiogenic stress |
| 1.2.3.4 | oxalate oxidase |
analysis |
membrane inlet mass spectrometry assay to directly measure initial rates of carbon dioxide formation and oxygen consumption in the presence and absence of hydrogen peroxide |
| 1.2.5.3 | aerobic carbon monoxide dehydrogenase |
analysis |
construction of an enzyme-electrode based on carbon monoxide dehydrogenase (CODH) containing molybdenum (Mo) and copper (Cu), flavin adenine dinucleotide (FAD) and two different [2Fe-2S] clusters as cofactors, as a platform for dissolved CO concentration monitoring. The immobilized CODHs on Au electrode retain their catalytic activity and demonstrate changes to cyclic voltammetry and amperometry signals upon interactions with various dissolved CO. CODHs are capable of direct electron transfer without any mediator |
| 1.2.7.1 | pyruvate synthase |
analysis |
biochemical assay for activity, low-potential electrons are introduced by photochemical reduction of EDTA/deazaflavin and the generated pyruvate is trapped by chemical derivatization with semicarbazide. The product of CO2 fixation can be detected as pyruvate semicarbazone by HPLC-MS |
| 1.2.7.4 | anaerobic carbon-monoxide dehydrogenase |
analysis |
assay method for enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase based on membranes containing high levels of CO-induced hydrogenase |
| 1.2.7.5 | aldehyde ferredoxin oxidoreductase |
analysis |
in situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes that model the proposed active-site structure for the AOR family of tungsten enzymes. The complexes are characterized by UV-vis, electrospray ionization mass spectrometry, IR, and resonance Raman spectroscopies and are found to mimic the coordination environment including the W=E (E=O, S) bond strengths and hydrolytic reactions of the tungsten center of the AOR family |
| 1.2.7.8 | indolepyruvate ferredoxin oxidoreductase |
analysis |
development of an effective affinity chromatography technique |
| 1.2.7.11 | 2-oxoacid oxidoreductase (ferredoxin) |
analysis |
biochemical assay for activity, low-potential electrons are introduced by photochemical reduction of EDTA/deazaflavin and the generated pyruvate is trapped by chemical derivatization with semicarbazide. The product of CO2 fixation can be detected as pyruvate semicarbazone by HPLC-MS |
| 1.3.1.1 | dihydropyrimidine dehydrogenase (NAD+) |
analysis |
high performance liquid chromatography method for quantification of dihydrouracil to uracil ratio in plasma and application in screening for dihydropyrimidine dehydrogenase deficiency in patients treated with 5-fluorouracil. Plasma dihydrouracil to uracil ratio values are highly correlated with the plasma 5-fluorouracil-half-life values and are significantly associated with the toxic side effects, whereas, data set provided from genetic analysis of the coding sequences of the DPD gene are found to be insufficient to explain all the cases of the 5-fluorouracil-related toxicity pattern. Assay is suitable for routine clinical use for dihydropyrimidine dehydrogenase deficiency assessment in patients prior to 5-fluorouracil administration |
| 1.3.1.2 | dihydropyrimidine dehydrogenase (NADP+) |
analysis |
study on DPD enzyme expression using RT-PCR, immunohistochemistry, enzymatic activity and ELISA. Highest correlation is observed between protein expression measured by ELISA and enzyme activity, correlation of gene expression and ELISA is also significant |
| 1.3.1.9 | enoyl-[acyl-carrier-protein] reductase (NADH) |
analysis |
construction of tetracysteine-tagged enzyme variants carrying the tag at the N-terminus, C-terminus, or both N- and C-terminus. All the tetracysteine-tagged FabI enzymes have high enzyme activities while the enhanced green fluorescent protein-tagged FabI exhaustively loses the activity. The binding between 4',5'-bis(1,3,2-dithioarsolan-2-yl)fuorescein, i.e. FlAsH reagent and tetracysteine motif is stable against high pressure, high field strength, high temperature, and ultrasound. A capillary zone electrophoresis system equipped with a laser-induced fluorescence detector has a detection limit of 10-16 M for the labeled proteins |
| 1.3.1.9 | enoyl-[acyl-carrier-protein] reductase (NADH) |
analysis |
development of a simple thermal shift assay, which does not use ACP-linked substrates, to determine the binding ability of triclosan to the enzyme's active site |
| 1.3.1.19 | cis-1,2-dihydrobenzene-1,2-diol dehydrogenase |
analysis |
Escherichia coli, which carry genes coding for benzene dioxygenase and benzene dihydrodiol dehydrogenase, can be used to monitor benzene pollution in environmental airsamples collected from an oil refinery. The procedures involving whole-cell bioassays determine the concentration of benzene through benzene dioxygenase activity, which allows for direct correlation of oxygen consumption, and through the benzene dihydrodiol dehydrogenase that causes catechol accumulation and restores NADH necessary for the activity of the first enzyme. The assay is sensitive enough to detect the benzene vapor at a concentration level of 0.01 mM in about 30 min. The assay is applicalble to on-line monitoring of benzene concentration, no particular treatment of environmental samples is required |
| 1.3.1.22 | 3-oxo-5alpha-steroid 4-dehydrogenase (NADP+) |
analysis |
assay for evaluating 5alpha-reductase activity in large-scale clinical studies using the S9 fraction obtained by centrifugation of the homogenate supernatant at 9000 g for 30 min and gas chromatography-mass spectrometry |
| 1.3.1.22 | 3-oxo-5alpha-steroid 4-dehydrogenase (NADP+) |
analysis |
radiosubstrate in vitro incubation method for the determination of 5alpha-reductase type 1 activity using rat liver microsomes as an enzyme source |
| 1.3.1.33 | protochlorophyllide reductase |
analysis |
POR is an ideal model for studying catalysis near the solvent glass transition |
| 1.3.1.39 | enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) |
analysis |
sensitive assay method measuring the fluorescence decrease of NADPH as it is converted to NADP+ during the reaction, optimized for high-throughput screening |
| 1.3.1.70 | DELTA14-sterol reductase |
analysis |
partial purified enzyme suitable for reconstitution studies, reconstitution of isolated, soluble enzymes involved in cholesterol biosynthesis from lanosterol |
| 1.3.1.103 | 2-haloacrylate reductase |
analysis |
monitoring the production of (S)-2-chloropropionate from 2-chloroacrylate as a model system for monitoring NADPH availability. A phosphofructokinase pfkA pfkB double-deletion strain shows the highest yield of 2-chloropropionic acid product. The flux distribution of fructose-6-phosphate between glycolysis and the pentose phosphate pathway determines the amount of NAPDH available for reductive biosynthesis |
| 1.3.1.103 | 2-haloacrylate reductase |
analysis |
monitoring the production of (S)-2-chloropropionate from 2-chloroacrylate as a model system for monitoring NADPH availability. The presence of transhydrogenase UdhA increases product yield and NADPH availability while the presence of transhydrogenase PntAB has the opposite effect. A maximum product yield of 1.4 mol product/mol glucose is achieved aerobically in a Pnt-deletion strain with UdhA overexpression, a 150% improvement over the wild-type strain |
| 1.3.1.104 | enoyl-[acyl-carrier-protein] reductase (NADPH) |
analysis |
development of a simple thermal shift assay, which does not use ACP-linked substrates, to determine the binding ability of triclosan to the enzyme's active site |
| 1.3.3.3 | coproporphyrinogen oxidase |
analysis |
mass spectrometric assay for the two-step decarboxylative oxidation of coproporphyrinogen III to protoporphyrinogen IX catalyzed by CPO in mitochondria from human lymphocytes. The assay shows good reproducibility, uses simple workup by liquid-liquid extraction of enzymatic products, and employs commercially available substrates and internal standard. It was developed for use in clinical diagnostics of the inherited disorder hereditary coproporphyria |
| 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 |
| 1.3.3.5 | bilirubin oxidase |
analysis |
enzyme activity in serum bilirubin assays can be monitored by capillary electrophoresis |
| 1.3.3.5 | bilirubin oxidase |
analysis |
immobilized onto aminopropyl and arylamine glass beads to form an enzyme bioreactor |
| 1.3.3.5 | bilirubin oxidase |
analysis |
sandwich-type enzyme-amplified amperometric detection of DNA with ambient O2 as the substrate at neutral pH in the presence of chloride |
| 1.3.3.5 | bilirubin oxidase |
analysis |
application of polyammonium cations to enzyme-immobilized electrode: application as enzyme stabilizer for bilirubin oxidase |
| 1.3.3.5 | bilirubin oxidase |
analysis |
application of poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as enzyme stabilizer for bilirubin oxidase immobilized electrode |
| 1.3.3.5 | bilirubin oxidase |
analysis |
BOD has attracted considerable attention as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions |
| 1.3.3.5 | bilirubin oxidase |
analysis |
the ability to perform the oxygen reduction reaction under physiological conditions is the most interesting feature of the enzyme bilirubin oxidase in terms of the design of biocathodes for biofuel cell applications. The enzyme is commonly immobilized on a solid carrier to achieve the highest biocatalytic activity, stability, selectivity, and reusability. Optimization of the application of immobilized enzyme for direct electrocatalytic reduction of O2 |
| 1.3.3.6 | acyl-CoA oxidase |
analysis |
useful for the determination of free fatty acids |
| 1.3.3.6 | acyl-CoA oxidase |
analysis |
amperometric propionate sensor |
| 1.3.3.11 | pyrroloquinoline-quinone synthase |
analysis |
the gene pqqC is a suitable molecular marker that can be used complementary to housekeeping genes for studying the diversity and evolution of plant-beneficial pseudomonads |
| 1.3.7.5 | phycocyanobilin:ferredoxin oxidoreductase |
analysis |
construction of a plasmid containing genes of apo-allophycocyanin alpha-subunit without chromophore and chromophore synthetases HO1, i.e. ferredoxin-dependent heme oxygenase, and PcyA, i.e. phycocyanobilin:ferredoxin oxidoreductase, and expression in Escherichia coli. Holo-allophycocyanin, i.e. allophycocyanin alpha-subunit with chromophore, can be synthesized by autocatalysis in Escherichia coli. Recombinant holo-allophycocyanin alpha-subunit shows the same spectral and fluorescent properties as phycocyanin and serves as a good substitute for native phycocyanin for fluorescent tagging. Recombinant allophycocyanin alpha-subunit can inhibit hydroxyl and peroxyl radicals more strongly than holo-allophycocyanin alpha-subunit and native allophycocyanin |
| 1.3.7.8 | benzoyl-CoA reductase |
analysis |
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described |
| 1.3.8.7 | medium-chain acyl-CoA dehydrogenase |
analysis |
application of single exon and multiplex PCR protocol for sequencing based mutation screening of medium-chain acyl-CoA dehydrogenase and ornithine transcarbamylase genes. Both protocols give comparable resultswithout any re-design of the PCR primers or other optimization steps |
| 1.3.98.1 | dihydroorotate dehydrogenase (fumarate) |
analysis |
protocol to measure enzyme kinetic parameters based on isothermal titration calorimetry. Presence of dimethyl sulfoxide at 10%, v/v and Triton X-100 at 0.5%, v/v seems to facilitate the substrate binding process with a small decrease in KM value |
| 1.3.99.6 | 3-oxo-5beta-steroid 4-dehydrogenase |
analysis |
determination of the concentration of chenodeoxycholic acid by an enzyme kit consisting of 3alpha-hydroxysteroid dehydrogenase, 3-keto-5beta-steroid-DELTA4-dehydrogenase, NAD+, nitroblue tetrazolium, diaphorase and some other reagents |
| 1.3.99.23 | all-trans-retinol 13,14-reductase |
analysis |
the mouse pluripotent P-19 cell metabolizes retinol to atRA and thus can be used in a cell-based screen for disruptors of the pathway. The disruption of the pathway is easily detected and quantitated, the P-19 cell provides an in vitro model system for identifying and exploring the mechanism of action of chemicals that interfere with the critical cellular pathway |
| 1.3.99.29 | phytoene desaturase (zeta-carotene-forming) |
analysis |
the engineered endogenous CrPDS L505F mutant is a dominant selectable marker for Chlamydomonas reinhardtii and possibly for other green algae |
| 1.4.1.1 | alanine dehydrogenase |
analysis |
determination of L-Ala |
| 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 |
| 1.4.1.1 | alanine dehydrogenase |
analysis |
an enzymatic assay system to eliminate or measure D-Ala, which is reported to affect the taste of seafoods or sake, is constructed using alanine racemase (L-AlaR from Synechocystis sp. PCC6803) and L-alanine dehydrogenase (L-AlaDH from Phormidium lapideum). Using the assay system, the D-Ala contents of 7 crustaceans, i. e. mosa shrimp (Argis lar, Mosaebi), spiny lebbeid (Lebbeus groenlandicus, Oniebi), deepwater prawn (Pandalus eous,Amaebi), flathead lobster (Ibacus ciliates, Uchiwaebi), snow crab (Chionoecetes opilio, Zuwaigani), red snow crab (Chionoecetes japonicus, Benizuwaigani), and horsehair crab (Erimacrus isenbeckii, Kegani), are determined |
