The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.
Any of a variety of procedures which use biomolecular probes to measure the presence or concentration of biological molecules, biological structures, microorganisms, etc., by translating a biochemical interaction at the probe surface into a quantifiable physical signal.
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.
Exclusive legal rights or privileges applied to inventions, plants, etc.
The utilization of an electrical current to measure, analyze, or alter chemicals or chemical reactions in solution, cells, or tissues.
Determination of the quantity of a material present in a mixture by measurement of its effect on the electrical conductivity of the mixture. (Webster, 3d ed)
Arginine derivative which is a substrate for many proteolytic enzymes. As a substrate for the esterase from the first component of complement, it inhibits the action of C(l) on C(4).
Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
Incorporation of biotinyl groups into molecules.
A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Compounds consisting of glucosamine and lactate joined by an ether linkage. They occur naturally as N-acetyl derivatives in peptidoglycan, the characteristic polysaccharide composing bacterial cell walls. (From Dorland, 28th ed)
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
The N-acetyl derivative of glucosamine.
An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The rate dynamics in chemical or physical systems.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A basis of value established for the measure of quantity, weight, extent or quality, e.g. weight standards, standard solutions, methods, techniques, and procedures used in diagnosis and therapy.
The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.
A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.
A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.
The variety of all native living organisms and their various forms and interrelationships.
A worm-like blind tube extension from the CECUM.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
Specifications and instructions applied to the software.
The genetic complement of MITOCHONDRIA as represented in their DNA.
Substances that contain a fused three-ring moiety and are used in the treatment of depression. These drugs block the uptake of norepinephrine and serotonin into axon terminals and may block some subtypes of serotonin, adrenergic, and histamine receptors. However the mechanism of their antidepressant effects is not clear because the therapeutic effects usually take weeks to develop and may reflect compensatory changes in the central nervous system.
A metabolite of AMITRIPTYLINE that is also used as an antidepressive agent. Nortriptyline is used in major depression, dysthymia, and atypical depressions.
Tricyclic antidepressant with anticholinergic and sedative properties. It appears to prevent the re-uptake of norepinephrine and serotonin at nerve terminals, thus potentiating the action of these neurotransmitters. Amitriptyline also appears to antagonize cholinergic and alpha-1 adrenergic responses to bioactive amines.
The prototypical tricyclic antidepressant. It has been used in major depression, dysthymia, bipolar depression, attention-deficit disorders, agoraphobia, and panic disorders. It has less sedative effect than some other members of this therapeutic group.
A tricyclic dibenzazepine compound that potentiates neurotransmission. Desipramine selectively blocks reuptake of norepinephrine from the neural synapse, and also appears to impair serotonin transport. This compound also possesses minor anticholinergic activity, through its affinity to muscarinic receptors.
A tricyclic antidepressant similar to IMIPRAMINE that selectively inhibits the uptake of serotonin in the brain. It is readily absorbed from the gastrointestinal tract and demethylated in the liver to form its primary active metabolite, desmethylclomipramine.
A dibenzoxepin tricyclic compound. It displays a range of pharmacological actions including maintaining adrenergic innervation. Its mechanism of action is not fully understood, but it appears to block reuptake of monoaminergic neurotransmitters into presynaptic terminals. It also possesses anticholinergic activity and modulates antagonism of histamine H(1)- and H(2)-receptors.

Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. (1/550)

The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle, this protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of post-translational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the post-translational attachment of biotin to a single lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit of acetyl-CoA carboxylase, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxy-biotinylated form of BCCP interacts with transcarboxylase in the transfer of the carboxylate to acetyl-CoA to form malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. The NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment (residue 70-156) of BCCP (holoBCCP87) and the crystal structure of the biotinylated form of a C-terminal fragment (residue 77-156) of BCCP from Escherichia coli acetyl-CoA carboxylase have previously been determined. Comparative analysis of these structures provided evidence for small, localized conformational changes in the biotin-binding region upon biotinylation of the protein. These structural changes may be important for regulating specific protein-protein interactions. Since the dynamic properties of proteins are correlated with local structural environments, we have determined the relaxation parameters of the backbone 15N nuclear spins of holoBCCP87, and compared these with the data obtained for the apo protein. The results indicate that upon biotinylation, the inherent mobility of the biotin-binding region and the protruding thumb, with which the biotin group interacts in the holo protein, are significantly reduced.  (+info)

Dietary thiamin level influences levels of its diphosphate form and thiamin-dependent enzymic activities of rat liver. (2/550)

This study was prompted by our incomplete understanding of the mechanism responsible for the clinical benefits of pharmacological doses of thiamin in some patients with maple syrup urine disease (MSUD) and the question of whether thiamin diphosphate (TDP), a potent inhibitor of the activity of the protein kinase that phosphorylates and inactivates the isolated branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex, affects the activity state of the complex. Rats were fed a chemically-defined diet containing graded levels of thiamin (0, 0.275, 0.55, 5.5, and 55 mg thiamin/kg diet). Maximal weight gain was attained over a 3-wk period only in rats fed diets with 5.5 and 55 mg thiamin/kg. Feeding rats the thiamin-free diet for just 2 d caused loss of nearly half of the TDP from liver mitochondria. Three more days caused over 70% loss, an additional 3 wk, over 90%. Starvation for 2 d had no effect, suggesting a mechanism for conservation of TDP in this nutritional state. Mitochondrial TDP was higher in rats fed pharmacological amounts of thiamin (55 mg thiamin/kg diet) than in rats fed adequate thiamin for maximal growth. Varying dietary thiamin had marked but opposite effects on the activities of alpha-ketoglutarate dehydrogenase (alpha-KGDH) and BCKDH. Thiamin deficiency decreased alpha-KGDH activity, increased BCKDH activity, and increased the proportion of BCKDH in the active, dephosphorylated, state. Excess dietary thiamin had the opposite effects. TDP appears to be more tightly associated with alpha-KGDH than BCKDH in thiamin-deficient rats, perhaps denoting retention of alpha-KGDH activity at the expense of BCKDH activity. Thus, thiamin deficiency and excess cause large changes in mitochondrial TDP levels that have a major influence on the activities of the keto acid dehydrogenase complexes.  (+info)

Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. (3/550)

l-Aspartate oxidase is the first enzyme in the de novo biosynthesis of pyridinic coenzymes in facultative aerobic organisms. The enzyme is FAD dependent and it shares common features with both the oxidase and the fumarate reductase classes of flavoproteins. In this report we focused our attention on the supersecondary structure of the molecule by means of limited proteolysis studies. Moreover the polymerization state of the protein at different pH and the interactions with NAD and its analogues are described. The results suggest that l-aspartate oxidase is a monomer at pH values lower than 4.5 and a dimer at pH values higher than 6.5. The protein is organized in two major domains connected by a flexible loop located in the 120-140 region. The data obtained by limited proteolysis of the holo and the apo form in the presence and in the absence of substrates (fumarate and menadione), inhibitors (succinate) and NAD allows the proposition that both domains are involved in the binding of the flavin coenzyme. Moreover the data reported in this manuscript suggest that NAD inhibits l-aspartate oxidase activity by competing with the flavin for the binding to the enzyme.  (+info)

Effects of divalent metal ions on the activity and conformation of native and 3-fluorotyrosine-PvuII endonucleases. (4/550)

The activities of restriction enzymes are important examples of Mg(II)-dependent hydrolysis of DNA. While a number of crystallographic studies of enzyme-DNA complexes have also involved metal ions, there have been no solution studies exploring the relationship between enzyme conformation and metal-ion binding in restriction enzymes. Using PvuII restriction endonuclease as a model system, we have successfully developed biosynthetic fluorination and NMR spectroscopy as a solution probe of restriction-enzyme conformation. The utility of this method is demonstrated with a study of metal-ion binding by PvuII endonuclease. Replacement of 74% (+/- 10%) of the Tyr residues in PvuII endonuclease by 3-fluorotyrosine produces an enzyme with Mg(II)-supported specific activity and sequence specificity that is indistinguishable from that of the native enzyme. Mn(II) supports residual activity of both the native and fluorinated enzymes; Ca(II) does not support activity in either enzyme, a result consistent with previous studies. 1H- and 19F-NMR spectroscopic studies reveal that while Mg(II) does not alter the enzyme conformation, the paramagnetic Mn(II) produces both short-range spectral broadening and longer range changes in chemical shift. Most interestingly, Ca(II) binding perturbs a larger number of different resonances than Mn(II). Coupled with earlier mutagenesis studies that place Ca(II) in the active site [Nastri, H. G., Evans, P.D., Walker, I.H. & Riggs, P.D. (1997) J. Biol. Chem. 272, 25761-25767], these data suggest that the enzyme makes conformational adjustments to accommodate the distinct geometric preferences of Ca(II) and may play a role in the inability of this metal ion to support activity in restriction enzymes.  (+info)

The aconitase of yeast. V. The reconstitution of yeast aconitase. (5/550)

The apoenzyme of yeast aconitase [EC 4.2.1.3] was prepared by treatment of yeast aconitase with sodium mersalyl, followed by passage by passage of the reaction mixture through a column of Dowex A-1 and gel filtration on Sephadex G-25. The apoenzyme had no aconitase activity, but the active enzyme could be reconstituted by treatment of the apoenzyme with ferrous ions and sodium sulfide in the presence of 2-mercapto-ethanol. The reconstituted active enzyme was isolated by DEAE-Sephadex A-50 column chromatography and Sephadex G-100 gel filtration from the reaction mixture. The reconstituted enzyme was identical with the original untreated enzyme in terms of specific activity, iron content and spectral characteristics, but not in terms of labile sulfur content. A significant difference in visible spectra between the holo- and apoenzymes appeared to be due to the difference in iron and labile sulfur contents between the two proteins.  (+info)

Rapid PCR test for discriminating between Candida albicans and Candida dubliniensis isolates using primers derived from the pH-regulated PHR1 and PHR2 genes of C. albicans. (6/550)

The development of a satisfactory means to reliably distinguish between the two closely related species Candida albicans and Candida dubliniensis in the clinical mycology laboratory has proved difficult because these two species are phenotypically so similar. In this study, we have detected homologues of the pH-regulated C. albicans PHR1 and PHR2 genes in C. dubliniensis. Restriction fragment length polymorphism analysis suggests that there are significant sequence differences between the genes of the two species. In order to exploit this apparent difference, oligonucleotide primers based on the coding sequence of the C. albicans PHR1 structural gene were designed and used in PCR experiments. Use of these primers with C. albicans template DNA from 17 strains yielded a predicted 1.6-kb product, while C. dubliniensis template DNA from 19 strains yielded no product. We therefore propose that PCR using these primers is a rapid and reliable means of distinguishing the two germ tube- and chlamydospore-producing species C. albicans and C. dubliniensis.  (+info)

A novel 35 kDa frog liver acid metallophosphatase. (7/550)

The lower molecular weight (35 kDa) acid phosphatase from the frog (Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i. e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with geff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases.  (+info)

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors. (8/550)

The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli. A purification procedure, faster than the one used for the enzyme from the natural source (bDASPO), has been set up yielding about 2 mg of pure recombinant protein (rDASPO) per each gram of wet E. coli paste. rDASPO has been shown to possess the same general biochemical properties of bDASPO, except that the former contains only FAD, while the latter is a mixture of two forms, one active containing FAD and one inactive containing 6-OH-FAD (9-20% depending on the preparation). This results in a slightly higher specific activity (about 15%) for rDASPO compared to bDASPO and in facilitated procedures for apoprotein preparation and reconstitution. Redox potentials of -97 mV and -157 mV were determined for free and l-(+)-tartrate complexed DASPO, respectively, in 0.1 M KPi, pH 7.0, 25 degrees C. The large positive shift in the redox potential of the coenzyme compared to free FAD (-207 mV) is in agreement with similar results obtained with other flavooxidases. rDASPO has been used to assess a possible oxidative activity of the enzyme towards a number of compounds used as agonists or antagonists of neurotransmitters, including d-aspartatic acid, d-glutamic acid, N-methyl-d-aspartic acid, d,l-cysteic acid, d-homocysteic acid, d, l-2-amino-3-phosphonopropanoic acid, d-alpha-aminoadipic acid, d-aspartic acid-beta-hydroxamate, glycyl-d-aspartic acid and cis-2, 3-piperidine dicarboxylic acid. Kinetic parameters for each substrate in 50 mM KPi, pH 7.4, 25 degrees C are reported.  (+info)

The invention discloses a device and method by which dry reagent enzyme based electrochemical biosensors, which are in a relatively mature form due to the extensive amount of development pioneered by the blood glucose monitoring industry, may be simply adapted to perform tests for blood coagulation, enzymatic activity, or immunochemical assays for antigens present in a fluid sample. In particular, the utility of combining apoenzyme based dry reagent electrochemical biosensors with apoenzyme reactivation technology is taught. This combination creates a novel combination test technology capable of detecting a wide range of different analytes, and operating in a wide variety of wet or dry, in vivo or in vitro environments.
NEET 2017 Biology solution (With NCERT Reference) 1. Which one of the following statements is correct, with reference to enzymes? Holoenzyme = Apoenzyme + Coenzyme Coenzyme = Apoenzyme + Holoenzyme Holoenzyme = Coenzyme + Co-factor Apoenzyme = Holoenzyme + Coenzyme Ans. (1) [NCERT 11th Page 159] 2. A decrease in blood pressure / volume will…
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Salmonella typhimurium encounters a variety of acid conditions during both its natural and pathogenic existence. The ability of this organism to respond transcriptionally to low pH is an area of active interest but little knowledge. As part of an ongoing investigation of low-pH adaptation, 18 pH-con …
3 3 THEN 330 280 L P r e v = L t 290 B i t e = l 300 D i f f e r i t = l . 0 E - 4 310 Mprev=Mt 320 GO TO 360 330 LPrev=10OE-6 340 D i f f c r i t = l . O05 360 MPrev=Mt 370 REM * I * ITERATION LOOP BEGINS * * * 380 M f r e e = M t / ( l + K l * L P r e v ÷ B 2 * L P r e v ~ 2 + B 3 * L P r e v ~ 3 ) 390 M l = M f r e e * K l * L P r e v 400 M l 2 = M f r e e * B 2 * L ~ r e v ~ 2 410 M13=Mfree*B3*LPrev~3 420 L ? r e e = L t - M I - 2 * M 1 2 - 3 * M 1 3 430 L d i f ? = L ? r e e - L P r e v 440 L P r e v = L P r e v ÷ B i t e * L d i ? Vallee, this series, Vol. 54, p. 446. [5] METAL-FREE ENZYMES 23 Special attention should be given to the chemical composition of solutions to be used for preparation and reconstitution of apoenzymes. Many of the buffers commonly employed are also metal-chelating agents at biological pH ranges. , cobalt. HEPES, a sulfonic acid derivative, has been successfully used as a buffer salt to prepare a number of apoenzymes. Metal-buffer binding constants of G o o d ...
PHR1山羊多克隆抗体(ab85706)可与大鼠样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
Shop L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase ELISA Kit, Recombinant Protein and L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
CRY1_CULQU (B0WRR9 ), CRY1_SINAL (P40115 ), CRY2_ARATH (Q96524 ), CRY2_VIBCH (Q9KS67 ), CRYD_GLOVI (Q7NMD1 ), CRYD_OSTTA (Q5IFN2 ), CRYD_RHOBA (Q7UJB1 ), CRYD_SYNY3 (P77967 ), PHRA_AGRFC (A9CJC9 ), PHR_BACPE (Q04449 ), PHR_BUCAI (P57386 ), PHR_BUCBP (Q89AJ9 ), PHR_ECOLI (P00914 ), PHR_HALSA (Q9HQ46 ), PHR_NEUCR (P27526 ), PHR_SALTY (P25078 ), PHR_STRGR (P12768 ), PHR_SYNP6 (P05327 ), PHR_SYNY3 (Q55081 ), PHR_THET2 (P61496 ), PHR_THET8 (P61497 ), PHR_VIBCH (Q9KNA8 ), PHR_YEAST (P05066 ...
NO diffuses to the adjacent smooth muscle where it interacts with different receptor molecules, of which the sGC is the best characterized and presumably most important one with regard to control of vessel tone and smooth muscle proliferation. The catalytically active holoenzyme exists as an obligate heterodimer consisting of 1 α and 1 β subunit and a noncovalently bound ferrous heme.9 The most abundant isoform in mammalian tissues is the α1 (73 to 78 kDa)/β1 (70 kDa) heterodimer. Significant protein expression of 2 other homologues subunits has only been detected in the human placenta (α2)10,11 and kidney (β2).12 At the genomic level, a dominant-negative splice variant of α2 classified as α2i has been detected.13 The interspecies homology of the individual subunits is high, whereas the intersubunit homology is lower.14 In contrast to α1 and β1, the biological significance of α2, α2I, and β2 is still obscure. The α2 subunit has recently been shown to be linked to cerebral ...
Antitoxic Unit [Ger. Antitoxineinheit]; Apoenzyme; Aryepiglottic; Atherosclerotic Encephalopathy; Atrial Ectopic [heart Beat]; Avian ...
Plasmid pHR iSH-YFP-PIF from Dr. Wendell Lims lab contains the inserts p85 iSH2 and PIF6 1-100 and is published in Nat Methods. 2011 Sep 11;8(10):837-9. doi: 10.1038/nmeth.1700. This plasmid is available through Addgene.
command in MATLAB. You can launch a pre-configured optimization task in Response Optimization Tool by first opening the model and by double-clicking on the orange block at the bottom of the model. From the Response Optimization Tool, press the Plot Model Response button to simulate the model and show how well the initial design satisfies the design requirements.. ...
1HVA: Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form.
1AH4: A specificity pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
Difluoro-oxaloacetate interacts with the aldimine form of aspartate transaminase to give a complex, the dissociation constant of which has been determined spectrophotometrically and by 19F n.m.r. (nuclear magnetic resonance). The 19F n.m.r. line-width-pH and chemical-shift-pH profiles of difluoro-oxaloacetate in the presence of the aldimine form of the enzyme both show inflexion points in the pH5 and pH8 regions, which may arise from variations in the binding of difluoro-oxaloacetate as specific groups on the enzyme are successively protonated. Difluoro-oxaloacetate also interacts with apoenzyme to form a complex, the dissociation constant of which was determined by 19F n.m.r. The 19F n.m.r. line-width-pH and chemical-shift-pH profiles of difluoro-oxaloacetate in the presence of apoenzyme show a single inflexion point in the region of pH8. The absence, in this case, of an inflexion in the pH5 region indicates that the latter, present in the corresponding profiles for the aldimine form of the ...
Ured by gamma counting from 16 weeks. The fold changes were 2.19, 2.72, and 3.65 (p,0.001) for 16, 24, and 32 weeks, respectively, compared to the 0 weeks
Regulation of the expression of the gene(s) coding for the 78-kD, biotin-containing subunit of [beta]-methylcrotonyl-coenzyme A carboxylase (MCCase) was investigated in different organs of tomato (Lycopersicon esculantus) plants. The specific activity of MCCase is highest in extracts from roots, followed in descending order by ripe and ripening fruits, stems, and leaves. The specific activity is 10-fold higher in roots than in leaves. However, the steady-state levels of the 78-kD subunit of MCCase and its mRNA are approximately equal in both roots and leaves. Instead, the difference in MCCase activity between these two organs is directly correlated to the biotinylation status of the enzymes biotin-containing subunit. Thus, the lower activity of MCCase in leaves is attributed to the reduced biotinylation of the biotin-containing subunit of the enzyme. Consistent with this model, a pool of nonbiotinylated enzyme is present in leaves, whereas the nonbiotinylated enzyme is undetectable in roots. ...
dUTPases are housekeeping enzymes which catalyse the hydrolysis of dUTP to dUMP in an ion-dependent manner. Bacillus subtilis has both a genomic and an SPβ prophage homotrimeric dUTPase. Here, structure determination of the prophage apoenzyme and of its complexes with dUDP and dUpNHpp-Mg(2+) is
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youtube]http://www.youtube.com/watch?v=jzIBZQkj6SY[/youtube] Once again our overseas brethren prove that their marketing creativity knows no bounds with a real life Angry Birds demonstration in Barcelona. This was set up on May 11th and its been making the internet rounds ever since and by popular demand were finally getting it posted. So enjoy the 1:41 of pure Angry Birds fun and try to remember that while we in America never get to do anything this fun for T-Mobile marketing, … [read full article]. ...
This Valentines weekend some American zoos are offering an adults-only opportunity to discover animals amorous antics, and perhaps pick up a few tips.
Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Catalysis involves the formation of a Schiffs base intermediate formed at the epsilon-amino group of Lys229. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved structural results that are less subject to model bias. Crystals were also soaked with the natural substrate (fructose 1,6-bisphosphate), and the crystal structure of this complex has been determined to 2.8 A. The apo structure differs from the previous Brookhaven-deposited structure (1ald) in the flexible C-terminal region. This is also the region where the native and complex structures exhibit differences. The conformational changes between native and complex structure are not large, but the observed complex does ...
Citation: Lee, L.F., Silva, R.F., Heidari, M., Reddy, S. 2010. Studies on Mareks Disease Virus Encoded Ribonucleotide Reductase. American Association of Avian Pathologists Symposium and Scientific Program, August 1-4, 2010, Atlanta, Georgia. Paper No. 9410-2. Interpretive Summary: Technical Abstract: Ribonucleotide reductase (RR) is an essential enzyme for the conversion of ribonucleotides to deoxyribonucleotides in prokaryotic and eukaryotic cells. The enzyme consists of two subunits namely RR1 and RR2, both of which associate to form an active holoenzyme. Herpesviruses express a functional RR required for viral pathogenesis and reactivation from latency in infected host. In pseudorabies virus, mutants deficient in RR were shown to be avirulent for pigs and capable for protecting pigs against disease. Mareks disease virus (MDV) also encodes a RR enzyme, which has 21 discrete blocks of amino acid homologous to other herpes viruses. These homologous blocks of amino acids are important sites for ...
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
The aim of this study was to identify the cardiac oxidoreductases involved in the metabolism of 4-hydroxy-2-trans-nonenal (HNE), an α,β unsaturated aldehyde generated during the peroxidation of ω-6 polyunsaturated fatty acids. In homogenates of bovine, human and rat ventricles the primary pyridine coenzyme-linked metabolism of HNE was associated with NADPH oxidation. The NADPH-dependent enzyme catalysing HNE reduction was purified to homogeneity from bovine heart. The purified enzyme displayed kinetic and immunological properties identical with the polyol pathway enzyme aldose reductase (AR), and catalysed the reduction of HNE to its alcohol 1,4-dihydroxynonene (DHN), with a Km of 7±2 μM. In the presence of NADP the enzyme did not catalyse the oxidation of DHN. During catalysis, HNE did not cause inactivation of AR. Nevertheless when the apoenzyme was incubated with HNE a dissociable complex was formed between the enzyme and HNE, followed by irreversible loss of activity. Inactivation of ...
Complete information for HCCS gene (Protein Coding), Holocytochrome C Synthase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase ...
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Apoenzymes become active enzymes on addition of a cofactor. Cofactors can be either inorganic (e.g., metal ions and iron-sulfur ... An apoenzyme (or, generally, an apoprotein) is the protein without any small-molecule cofactors, substrates, or inhibitors ...
Nair PM, Vining LC (February 1965). "Isophenoxazine synthase apoenzyme from Pycnoporus coccineus". Biochimica et Biophysica ...
I. Purification of the apoenzyme and synthetase; characteristics of the reaction". J. Biol. Chem. 239: 2858-2864. Biology ...
However, the apoenzyme without copper is unstable. Apoceruloplasmin is largely degraded intracellularly in the hepatocyte and ...
Groen BW, van Kleef MA, Duine JA (March 1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni ...
Methylmalonyl-CoA mutase is a mitochondrial homodimer apoenzyme (EC. 5. 4.99.2) that focuses on the catalysis of methylmalonyl ...
Molecular size of the D-amino acid oxidase apoenzyme subunit". J. Biol. Chem. 244 (2): 465-470. PMID 4388073. Pettigrew DW, ...
Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme". The Journal of Biological Chemistry. ...
A complex of the apoenzyme and citrate at 1.87 A resolution". Journal of Molecular Biology. 226 (3): 867-82. doi:10.1016/0022- ...
Crystallographic studies have helped elucidate the apoenzyme structure of phosphopentose epimerase. Results of these studies ...
Recny MA, Hager LP (November 1982). "Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD ...
"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli". Journal of Molecular ...
"Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD". J. Biol. Chem. 257 (21): 12878-86 ...
2. Spectroscopic Studies on the Apoenzyme and the Monomeric and Dimeric Forms". European Journal of Biochemistry. 33 (2): 271-8 ...
Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An enzyme together with the ...
If an enzyme needs coenzyme to work itself, it is called an apoenzyme. In fact, it alone cannot catalyze reactions properly. ...
Before addition of the pyridoxal phosphate cofactor, the apoenzyme exists in an open conformation. Upon cofactor binding, a ...
Kamei S, Ohkubo A, Yamanaka M (1979). "Apoenzyme of aspartate aminotransferase isozymes in serum and its diagnostic usefullness ...
... preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Arch. Biochem. Biophys. 337 (1): 89-95. doi: ...
Qi D.F., Wang Y.L., "Studies on Succinic Dehydrogenase V, The Linking between the Flavin Prosthetic Group and the Apoenzyme, ... Wang, Y.L. (1966). "Studies on Succinic Dehydrogenase, Purification, Properties and Linking between the Apoenzyme and the ...
... preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Archives of Biochemistry and Biophysics. 337 ...
... and the properties of the apoenzyme subunits". Acta Biochim. Pol. 13 (4): 311-28. PMID 5962440. SMILEY KL, SOBOLOV M (1962). "A ...
Dewanti AR, Duine JA (May 1998). "Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ ...
... the binding process of PQQ to the apoenzymes". Biosci. Biotechnol. Biochem. 59: 1548-1555. doi:10.1271/bbb.59.1548. Soluble+ ...
Apoenzymes can still bind glucose but, due to the lack of cofactors (in vitro), cannot catalyse their reaction so are less ... This protein has also been used in fluorescent sensing either simply as an apoenzyme or as a holoenzyme. An exception to this ... Chinnayelka, S. and M.J. McShane, RET nanobiosensors using affinity of an apo-enzyme toward its substrate. Conf Proc IEEE Eng ... but then switching to GOx apoenzyme in 2004 (TRITC-apo-GOx /FITC-dextran (500kDa)), and in 2009 testing sensors (QSY-21-apo-GOx ...
The apoenzyme, not active and bound to substrates, has an acidic isolelectric point of pH 5.0-5.2. Unusual for proteins, this ...
Three of these were of the wild type: the apoenzyme in 1S2T, the enzyme plus its magnesium ion cofactor in 1S2V, and the enzyme ... A mutant (D58A, in one of the active-site loops) was crystallized as an apoenzyme also (1S2U). From these structures, an active ...
In this system, the inactive form (the apoenzyme) becomes the active form (the holoenzyme) when the coenzyme binds. In the ...
This changes the active site from an open cleft in the apo-enzyme into a nearly solvent inaccessible pocket. This theme of ... Structural studies of P. aeruginosa PMM/PGM by X-ray crystallography have been conducted as both apo-enzyme and as protein- ...
An inactive enzyme without the cofactor is called an apoenzyme, while the complete enzyme with cofactor is called a holoenzyme ...
In particular, the utility of combining apoenzyme based dry reagent electrochemical biosensors with apoenzyme reactivation ... These PQQ apoenzyme prosthetic groups, in turn, bind to the electrode-bound GDH apoenzyme, and change the GDH apoenzyme into an ... the apoenzyme (4), (14) contains a reagent form of the antigen (9), (19) chemically coupled to apoenzyme (4), (14), and this ... Here the apoenzyme (1), which may be the apoenzyme form of glucose oxidase, or other enzyme, is mounted or otherwise associated ...
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad ... CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD ...
ENGINEERING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF THE HIS-94-, CYS APOENZYME IN A NEW CRYSTALLINE ... Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94Cys apoenzyme in a new crystalline ... CYS APOENZYME IN A NEW CRYSTALLINE FORM ...
Interaction of Proteus mirabilis Urease Apoenzyme and Accessory Proteins Identified with Yeast Two-Hybrid Technology. Susan R. ... The urease gene cluster of P. mirabilis encodes three structural polypeptides, UreA, UreB, and UreC, which form the apoenzyme; ... 4); UreD was arbitrarily drawn contacting the apoenzyme face opposite UreA; there is no direct evidence for this structure. ... It is likely that some accessory proteins require physical contact with their respective apoenzyme or other coaccessory ...
Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme. X. Wang, E. S. Wurtele, ... Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme ... Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme ... Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme ...
... - reactivation. immunoassay system), strips are impregnated with the dry conjugate , ... Meaning of "apoenzyme" in the English dictionary. To add the top layer to the sandwich, the FAD-conjugated monoclonal mouse ... Typically, apoenzyme 21 will contain prosthetic binding site 22 and the enzyme active site 23 which, in the absence of the ... An apoenzyme 4 containing an active site 5 and a prosthetic group binding site 6and an artificially coupled reagent-ligand ...
... - reactivation. immunoassay system), strips are impregnated with the dry conjugate , ... Synonyms and antonyms of apoenzyme in the English dictionary of synonyms. I do not know quite how to explain the apoenzyme data ... Here, as before, the electrochemical apoenzyme immuniassayimmunossay may be the apoenzyme form of glucose oxidase, or other ... Meaning of "apoenzyme" in the English dictionary. From here, the electrons may in turn pass into electrical conduits or traces ...
Rhymes for apoenzymes. Found with a strict rhyme search. Searched for rhymes at the end of the words. Rhymebox - the rhyming ... More about apoenzymes. Knowledge Wikipedia Wiktionary Google Images Google Yahoo! Flickr Videos Google Yahoo! Youtube ...
What is an apoenzyme?. A: Apoenzymes are proteins that form active enzyme systems by combining with coenzymes and establishing ...
What is an apoenzyme?. A: Apoenzymes are proteins that form active enzyme systems by combining with coenzymes and establishing ...
4.2 Apoenzyme/cofactor reconstitution. Even though biotin/(S)Av couples certainly exhibit nearly ideal features in terms of ... by Nolte and co-workers who took advantage of the strong interactions involved in the reconstitution between an apoenzyme and ... binding and host guest recognition process, the apoenzyme/cofactor reconstitution strategy represents an interesting ...
b) The apoenzyme is a part of all enzymes.. c) Proenzymes are active enzymes. ...
In addition, the quinone is hydrogen-bonded to a water molecule not present in the apo enzyme (W5 in Fig. 2B) that bridges the ... In this paper we report the apoenzyme structures of human (at 1.7-Å resolution) and mouse (2.8 Å) QR1 and the complex of the ... This is caused in part by the lack of structural information about the apoenzyme (apo) containing only the FAD prosthetic group ...
Conformational features of the holo- and apo-enzyme forms of serine hydroxymethyl transferase. Indian Journal of Biochemistry ... Conformational features of the holo- and apo-enzyme forms of serine hydroxymethyl transferase. ...
1). Cytochrome oxidase subunit I (CO1) and Cytochrome b apoenzyme (Cytb), the 2 most common mitochondrial gene sequences in ... Cytochrome b apoenzyme (Cytb); NADH dehydrogenase subunits 1 to 4 (ND1 to ND4), 4 L (ND4L), 5 (ND5), and 6 (ND6)-and 2 ...
Apo-Enzyme. 19.127 g 0.40%. 0.673. MU/g. pyrrolo-quinoline quinine. Co-Factor. 0.5329 g 0.01%. ...
Coordinate Synthesis of Heme and Apoenzyme in the Formation of Tryptophan Pyrrolase ...
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Flavodoxin); 0 (Holoenzymes); 0 (Multienzyme Complexes); 0 (Recombinant Fusion ...
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Benzoquinones); 0 (Carrier Proteins); 0 (Protein Aggregates); 0 (Recombinant ...
Worthington Tyrosine Decarboxylase, Apoenzyme [WLS004968-250MG] - UNSPSC Code(s):12352204Activates to at least 0.2 units per ... Worthington Tyrosine Decarboxylase, Apoenzyme. Price(USD):$109.20. *Ask Promo Code: Equl SKU. Product Name. UOM. Specification ...
E: apoenzyme; AdoCbl: adenosylcobalamin; S: substrate; P: product; RF: reactivase; AdoH: 5′-deoxyadenosine; Cbl: cobalamin or ...
a. Apoenzyme Reagents-1.5 μM apoglucose oxidase (U.S. Pat. No. 4,268,631), 100 μl/ml antiserum to glucose oxidase, 3.5 μl/ml ... Apoenzyme reactivation electrochemical detection method and assay. US9156787. Jul 24, 2014. Oct 13, 2015. Board Of Regents Of ... Apoenzyme reactivation electrochemical detection method and assay. US20070289880 *. Jan 22, 2007. Dec 20, 2007. Zweig Stephen E ... An apoenzyme reactivation immunoassay system (ARIS, see U.S. Pat. No. 4,238,565) was established for imipramine as follows:. 1 ...
Crystal structure of apoenzyme cAMP-dependent protein kinase catalytic subunit ... Crystal structure of apoenzyme cAMP-dependent protein kinase catalytic subunit; X-RAY DIFFRACTION 2.90 Å SMTL ID. 1j3h.1. ...
The holoenzyme was prepared by incubating the apoenzyme at 4°C for 30 min in 50 mM HEPES (pH 7.0) with 100 μM PQQ and 100 mM ... Solid line, apoenzyme; dashed line, oxidized holoenzyme; dotted line, reduced holoenzyme. The reduced form was prepared by ... 3). When the holoenzyme was prepared by incubating the apoenzyme with PQQ and CaCl2, followed by removal of excess additives, a ... The UV-visible (UV-Vis) absorption spectrum of the oxidized form of the holoenzyme, prepared by incubating the apoenzyme with ...
Study Set 16 Enzymes and Hormones flashcards from Languages 247365
Study Biological Molecules flashcards from Rachel Lorenzon
Data are shown from apoenzymes (A and E), in the presence of 1.5× Zn(II) (B and F), 1.5× Zn(II), and 10× Suc (C and G) or 1.5× ... A, D, and G, spectra of the apoenzymes shown in gray. B, E, and H, spectra of the enzymes in the presence of 1.5× Zn(II) and 10 ...
Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis ... Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis. Coordinates. PDB Format Method. X-RAY ...
Apoenzymes become active enzymes on addition of a cofactor. Cofactors can be either inorganic (e.g., metal ions and iron-sulfur ... An apoenzyme (or, generally, an apoprotein) is the protein without any small-molecule cofactors, substrates, or inhibitors ...
4-aminobutyrate aminotransferase apoenzyme. BACME. 451. UniRef100_A0A1Q8UZS4. 4-aminobutyrate--2-oxoglutarate transaminase. ...
  • 5. The device of claim 1 , in which said hydrolase analyte enzyme induced changes in the activity of said electrochemical apoenzyme is selected from the group consisting of enzyme cofactor addition, prosthetic group addition, allosteric regulator binding, covalent enzyme modification, or proteolytic cleavage. (google.com)
  • A holoenzyme refers to a catalytically active enzyme that consists of both apoenzyme (enzyme without its cofactor(s)) and cofactor. (wikibooks.org)
  • Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins . (cosmeticsandtoiletries.com)
  • The UV-visible (UV-Vis) absorption spectrum of the oxidized form of the holoenzyme, prepared by incubating the apoenzyme with PQQ and CaCl 2 , revealed a broad peak at approximately 350 nm, indicating that the enzyme binds PQQ. (asm.org)
  • they bind apoenzyme to proteins to produce an active holoenzyme . (wikibooks.org)
  • Cofactors with an apoenzyme are called a holoenzyme, which is the active form. (wikibooks.org)
  • 2,3-Butanedione (under room light), 8-anilinonaphthalenesulfonate, ethoxyformic anhydride and rosebengal (under irradiation with tungsten lamp) inactivated especially apoenzyme, and Arg and His residue are presumed to participate in the formation of holoenzyme complex. (springer.com)
  • These results suggest that both Cys and Tyr residues of apoenzyme bind directly to Ca 2+ in holoenzyme complex. (springer.com)
  • The stimulated activity with added in-vitro PALPO shows the level of holoenzyme plus apoenzyme. (oregonstate.edu)
  • 0.01), which indicated that the level of holoenzyme is largely dependent on the amount of-apoenzyme available. (oregonstate.edu)
  • wherein said complex is on a surface that is spatially separated from the region or regions of the apparatus where the apoenzyme or inactive form of said electrochemical enzyme are located. (google.com)
  • The liberated enzyme prosthetic group or other enzyme immunoassaj factor 36 can now bind to the prosthetic group region of apoenzyme The liberated apoglucose oxidase can then bind to the wired unbound FAD groups, reassociate, and then start generating an electrical signal that increases in response to higher levels of the test analyte. (yalasarat.info)
  • Typically, apoenzyme 21 will contain prosthetic binding site 22 and the enzyme active site 23 which, in the absence of the prosthetic group 13 will be in an inactive state. (yalasarat.info)
  • Similarly, if the test substrate 818 is a long chain carbohydrate such as glycogen, and the analyte enzyme 919 is a glycogen cleaving enzyme such as amylase, the amylase will also act to cleave the link and separate the prosthetic group 616 from the blocking group or surface 717again liberating the prosthetic group, reactivating apoenzyme 2131and producing a detectable signal. (yalasarat.info)
  • Here, as before, the electrochemical apoenzyme immuniassayimmunossay may be the apoenzyme form of glucose oxidase, or other enzyme, is mounted or otherwise associated with the surface of electrode 5. (kuzemkinomo.ru)
  • In the simplest form, the present invention discloses the utility of combining dry reagent electrochemical enzyme based biosensors with apoenzyme reactivation technology to produce a novel diagnostic test platform technology capable of detecting a wide range of analytes, and capable of operating in a dry or wet, in vivo or in vitro, environment. (kuzemkinomo.ru)
  • Apoglucose oxidase conjugated microbeads: Typically amplification enzyme substrate 14as well as other reaction chemicals coagulation initiators, buffers, viscosity modifying polymers, and apoenzyme stabilizing agents such as trehalose are also present. (kuzemkinomo.ru)
  • Apoenzymes are proteins that form active enzyme systems by combining with coenzymes and establishing system specificity for a substrate. (reference.com)
  • In this paper we report the apoenzyme structures of human (at 1.7-Å resolution) and mouse (2.8 Å) QR1 and the complex of the human enzyme with the substrate duroquinone (2.5 Å) (2,3,5,6-tetramethyl- p -benzoquinone). (pnas.org)
  • Enzymes without their necessary cofactors are called apoenzymes, which are the inactive form of an enzyme. (wikibooks.org)
  • Interestingly, the coupling of this network that is apparent in the apoenzyme appears to be reduced in the phosphorylated enzyme intermediate. (proteopedia.org)
  • The enzyme is also inhibited by Be(II), Bi(III) as well as excess Zn(II), while the apoenzyme is reactivated by Zn(II). (spie.org)
  • Molecular models were generated for the apoenzyme and p[NH]ppA-bound states in the C-terminal regions by docking of a model based on a crystal structure from a closely related enzyme. (biochemj.org)
  • 0.01) existed between the basal activity and percent stimulation of EGOT, which meant that the high enzyme activity level is usually associated with a high degree of saturation of the apoenzyme with PALPO. (oregonstate.edu)
  • In particular, the utility of combining apoenzyme based dry reagent electrochemical biosensors with apoenzyme reactivation technology is taught. (google.com)
  • 2. The device of claim 1 , in which said electrochemical apoenzyme is glucose oxidase, and the complex contains FAD as the prosthetic group or activation moiety. (google.com)
  • The use of antiserum to glucose oxidase in the apoenzyme reactivation immunoassay system (ARIS) is described. (yalasarat.info)
  • Such recombinant antibody-apoenzyme fusion proteins could be useful in a number of different types of electrochemical immunoassays. (kuzemkinomo.ru)
  • Inactive enzymes which are not bound to their cofactors are called Apoenzymes. (jagranjosh.com)
  • Here's the terminology that we use: COFACTORS: chemicals required by inactive apoenzymes to convert them into active enzymes. (bio.net)
  • This is caused in part by the lack of structural information about the apoenzyme (apo) containing only the FAD prosthetic group (apo QR1) or of QR1 with substrate (i.e., with no inhibitor). (pnas.org)
  • Coenzyme B12-dependent diol dehydratase: regulation of apoenzyme synthesis in Klebsiella pneumoniae (Aerobacter aerogenes) ATCC 8724. (ebi.ac.uk)
  • Recovery is believed to require absorption of new unoxidized B12 (and synthesis of new apoenzyme). (erowid.org)
  • The iron-containing hemin group is covalently bound to the glycoprotein apoenzyme. (mpbio.com)
  • COSUBSTRATES: weakly bound to the apoenzyme often at a specific site. (bio.net)
  • Examples are ATP, SAM, many vitamins, coenzyme A, THF, NADH, and ubiquinone (coenzyme Q). PROSTHETIC GROUPS: these are tightly bound to the apoenzyme and if they participate in the reaction they must be regenerated at every reaction cycle. (bio.net)
  • When antigenic test ligands 11 are added to the system, they compete for binding between the antigenic reagent ligand group 19 previously coupled to the apoenzyme 14breaking the bond between the antigenic reagent ligand group 19 and the antibody The next steps of the reaction are shown in 21immunoassay25262728 and These free FAD-antibodies bind to the apoglucose oxidase in the neighboring beads, creating active glucose oxidase. (yalasarat.info)
  • The percent stimulation represents the degree of saturation of apoenzyme with the coenzyme (Cavill and Jacobs, 1967). (oregonstate.edu)
  • Reacitvation apoenzyme stimulation test is a popular method for measuring vitamin B6. (kuzemkinomo.ru)
  • Size exclusion chromatography of the apoenzyme showed that the tetramer unfolds via the intermediate formation of dimers. (ias.ac.in)
  • Removal of iron from TPH produces an apoenzyme with low activity that can be reconverted to its highly active holo-form by the addition of ferrous iron. (jneurosci.org)
  • Apoenzymes 131 additionally contain amplification substrate-binding sites 3 and the area immediately behind In some situations, it may be advantageous to include multiple electrodes in a single test strip in order to obtain both positive high and negative low onboard controls for the reaction. (kuzemkinomo.ru)
  • Detection of Zn(II) by apoenzyme reactivation occurs down to 3 ppb. (spie.org)
  • The structure of the apoenzyme shows flexibility within the active site. (osti.gov)
  • Homogeneous apoenzyme reactivation immunoassay for thyroxin-binding globulin in serum. (yalasarat.info)
  • Molecular simulations of different holo and apoenzyme complexes of SSTR2 in the presence and absence of a lipid bilayer were performed, observed, and correlated with previously reported studies. (nature.com)
  • N-acetylimidazole showed similar effects on apoenzyme, the activity being restored by hydroxylamine-treatment of the inactivated apoenzyme. (springer.com)