Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyclonal antisera prepared against the purified NADH peroxidase from Streptococcus faecalis ATCC 9790 (Enterococcus hirae) do not cross-react with the ATCC 11700 enzyme. Comparative tryptic maps of the two proteins indicate that the differences in primary structures extend beyond those localized to respective antigenic epitopes. Alignments of the NH2-terminal and active-site cysteinyl peptide sequences of the two streptococcal peroxidases reveal identities of 50 and 67% in the respective overlap regions. Dithionite titrations of the ATCC 9790 enzyme reveal a separation in potentials (E2 - E1) for the nonflavin and flavin redox centers of 39 mV, a value nearly 50 mV lower than that observed with the ATCC 11700 peroxidase. Despite these changes in redox behavior NADH titrations of the ATCC 9790 enzyme give rise to both EH2 and EH2.NADH species as previously observed. The enzyme turnover number with hydrogen peroxide is approximately 60% that of the ATCC 11700 peroxidase; the ATCC 9790 peroxidase is also inhibited during turnover with ethyl hydroperoxide. These findings suggest that the flavoprotein NADH peroxidases may exhibit greater diversity among the group D streptococci than previously observed with the widely distributed enzymes of the related flavoprotein disulfide reductase class.
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PMID:Heterogeneity among the flavin-containing NADH peroxidases of group D streptococci. Analysis of the enzyme from Streptococcus faecalis ATCC 9790. 216 44

Present work describes a new property of HDL to act as a scavenger of O2- free radicals in vitro. This lipoprotein prevents both enzymic and non-enzymic generation of O2- anions as evidenced by inhibition of xanthine oxidase, peroxidase, peroxidation of pyrogallol and phenazine methosulphate-NADH reaction. Ascorbate stimulated MDA formation in microsomes has been shown to be suppressed by HDL and these effects are comparable with that of BHA.
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PMID:High density lipoprotein is a scavenger of superoxide anions. 217 36

The objective of the present study was to explore the mechanisms responsible for the strong, direct-acting mutagenicity of 2-naphthohydroxamic acid (NHA) for Salmonella typhimurium TA98. NHA was converted to its O-acetate (O-Ac-NHA) by acetyl-CoA, in the presence of competent or heat-treated cell-free bacterial preparations. O-Ac-NHA, which is more mutagenic than NHA, reacted nonenzymatically with tRNA in neutral solutions with retention of both the naphthyl and carbonyl groups in the products, but NHA did not react. Enzymatic sulfate conjugation was not demonstrated. TA98 cells converted NHA to 2-aminoaphthalene, presumably through a Lossen rearrangement following O-acetylation or conjugation by other metabolic pathways. TA98 cells reduced O-Ac-NHA to 2-naphthamide, and NADH and NADPH were shown to be cofactors for reduction in the presence of a cell-free bacterial preparation. Although horseradish peroxidase and H2O2 catalyzed the binding of these compounds to tRNA, no evidence of oxidation of NHA or O-Ac-NHA was obtained with H2O2 and cell-free preparations of TA98 or the cells themselves, as judged by the lack of formation of the peroxidative product, 2-naphthoic acid. Both NHA and O-Ac-NHA reacted with DNA of TA98 with retention of both naphthyl group and carbonyl of the naphthoyl moiety in the adduct(s). These results suggest that NHA may be activated in TA98 by esterification, and the resulting metabolites may amidate or carbamoylate nucleic acids.
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PMID:Metabolic activation of the potent mutagen, 2-naphthohydroxamic acid, in Salmonella typhimurium TA98. 219 54

Experiments are presented that confirm earlier predictions that the mode of supply of reactants to a nonlinear (bio)chemical reaction determines or controls concentrations at steady states far from equilibrium. The oxidation of nicotinamide adenine dinucleotide (NADH) catalyzed by the enzyme horseradish peroxidase with continuous input of oxygen was studied; NAD+ is continuously recycled to NADH through a glucose-6-phosphate dehydrogenase system. A comparison of steady-state concentrations is made with an oscillatory oxygen input and a constant input at the same average oxygen input for both modes. By varying the frequency and amplitude of the perturbation (O2 influx), the following may be changed: the average concentration of NADH; the Gibbs free energy difference delta G of the reactants and products at steady state; the average rate of the reaction; the phase relation between the oscillatory rate and delta G; and the dissipation. These results confirm the possibility of an "alternating current chemistry," of control and optimization of thermodynamic efficiency and dissipation by means of external variation of constraints in classes of nonlinear reactions and biological pumps, and of improvements of the yield in such reactions (heterogeneous catalysis, for example).
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PMID:Changes in mean concentration, phase shifts, and dissipation in a forced oscillatory reaction. 229 1

The conversion of pheromonal aldehydes to carboxylic acids in vitro in tissue extracts of Heliothis virescens is catalyzed by both aldehyde dehydrogenase and aldehyde oxidase enzymes. The aldehyde-oxidizing activity in antennae, heads, legs, and hemolymph from male and female moths was examined by radiochromatographic and spectroscopic assays. First, the enzymatic activity was measured in the presence or absence of added NAD+ using either (Z)-9-tetradecenal or (Z)-11-hexadecenal as tritiated substrate. Second, substrate specificity was determined spectroscopically by (i) indirect measurement of the AO-released hydrogen peroxide through the coupled AO-horseradish peroxidase reaction and by (ii) direct measurement of the ALDH-produced NADH. Both aldehyde-oxidizing activities were associated with soluble enzymes in the antennal extracts, and these enzymes degraded pheromone and nonpheromonal aldehydes. Both AO and ALDH activities were present in male and female tissues. AO activity was exhibited primarily in the antennal extracts and to a lesser degree in the leg extracts. Moreover, ALDH activity was distributed in the antenna, head, and leg extracts. A vinyl ketone analog of (Z)-11-hexadecenal preferentially inhibited the ALDH activity over the AO activity.
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PMID:Aldehyde-oxidizing enzymes in an adult moth: in vitro study of aldehyde metabolism in Heliothis virescens. 232 97

A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10% of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2- and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.
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PMID:Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata. 233 52

NADH oxidase activity has been detected at the ultrastructural level using cerium ions to trap H2O2 generated by the enzyme (via intermediate reactive oxygen species). In an attempt to localize NADH oxidase activity at the light microscope level using the cerium-diaminobenzidine (DAB)-nickel-H2O2, the cerium-DAB-cobalt-H2O2 or the cerium-alkaline lead procedures, the distribution patterns of the revealed enzyme were found to be identical to those for non-specific alkaline phosphatase and especially 5'-nucleotidase activity. With the cerium-DAB-cobalt-H2O2 visualization procedure, the distribution pattern of the final reaction product was similar to that obtained with the other two techniques but much less final reaction product was formed. Incubations for NADH oxidase activity performed in the presence of exogenous catalase or in the absence of catalase or peroxidase inhibitors did not affect the staining intensity, whereas inhibitors of 5'-nucleotidase (EDTA) and non-specific alkaline phosphatase (levamisole) always did. Therefore, phosphatases contribute to the formation of the final reaction product. Since NADH initially cannot be hydrolysed by either of these two phosphatases, then presumably nucleotide pyrophosphatase (E.C.3.6.1.9) cleaves NADH into 5'-AMP and nicotinamide mononucleotide in a first step. Both nucleotides can be hydrolysed further by the two monophosphatases. These then generate cerium phosphate which is detected by the DAB-nickel-H2O2, DAB-cobalt-H2O2 or lead visualization methods.
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PMID:Pitfalls in the light microscopical detection of NADH oxidase. 236 89

A sensitive staining method of horseradish peroxidase-labeled immunoglobulins on nitrocellulose membrane was established by employing a reaction chain leading to formazan formation with phenol as a substrate of peroxidase and NADH as a hydrogen donor to reduce nitro blue tetrazolium. Higher concentrations of NADH relative to phenol were necessary to increase the intensity of staining and to ensure a wide dose-response range of color production with respect to the applied enzyme activities. By an optimized tetrazolium method in combination with antibody-affinity blotting, as low as 4 ng/ml alpha-fetoprotein was detected and 3-4-fold greater color intensities in a working assay range as compared with those of existing methods were obtained. The present technique of peroxidase staining may prove to have a wide application for the enzyme immunoassay using blotting modalities.
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PMID:A tetrazolium method for staining peroxidase labels in blotting assays. 243 Oct 66

Previous studies have shown that behavioral and neurophysiological responses to tastes develop during rat's postnatal life. The present experiments evaluated morphological and metabolic development of neurons in the gustatory zone of the caudal parabrachial nucleus (PBNc) of rat. Histological reconstruction studies were conducted to establish coordinate systems for PBNc gustatory zones in developing rats. Reliability of coordinate systems were evaluated in separate experiments following infusions of horseradish peroxidase in the thalamic taste area. Morphological and Golgi impregnation studies were performed to characterize neuronal and dendritic architecture in PBNc gustatory zones defined by coordinates. Conventional histochemical studies were performed for the mitochondrial respiratory enzymes cytochrome C oxidase (CO; EC 1.9.3.1) succinate dehydrogenase (SDH; EC 1.3.99.1), and NADH-dehydrogenase (NADH-DH; EC 1.6.99.3). Results show that two somatic morphologies can be statistically characterized in PBNc gustatory zones: Multipolar somatic types and fusiform somatic types. Multipolar and fusiform neurons of neonatal and adult rats project axons to the thalamic taste area, and dendrites of these neurons grow extensively between approximately 16 days after birth to approximately 35 days after birth. Activity of CO, SDH, and NADH-DH increases in the PBNc gustatory zones during the period of dendritic growth, and continues to increase slightly to approximately 45 days. These results provide the first demonstration of postnatal morphological and metabolic developmental in a central gustatory relay. Postnatal development of gustatory system therefore appears similar to that reported for other sensory systems, to the extent that morphological and metabolic development accompanies the ontogeny of taste responses.
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PMID:Postnatal development of the parabrachial gustatory zone in rat: dendritic morphology and mitochondrial enzyme activity. 246 23

Morphological and metabolic development of the gustatory zone of the rostral nucleus of the solitary tract (NST) was examined in rat. Transganglionic transport of horseradish peroxidase (HRP) was used to visualize the organization of gustatory projections to the rostral gustatory NST in rats aged postnatal day 1 (P1) to P34. Golgi impregnation studies were performed to analyze morphological development of dendrites in regions of the rostral NST that were identified as anterior tongue terminal fields. Results demonstrate that afferent fibers of the anterior tongue project to the rostral NST in rats as young as P1. The volume of NST terminal fields increased from P1 to approximately P16-P20, and was adult-like after approximately P20. Developmental increases in terminal field volume resulted from a preferential expansion in the rostrocaudal plane. Planar length of first-order dendrites associated with fusiform, multipolar, and ovoid neurons, and second-order dendrites of fusiform and ovoid neurons, increased approximately three-fold between P4 and P16-20. First-order dendritic length for all morphological types was adult-like after approximately 20-25 days of age, whereas second-order dendritic length of multipolar neurons increased significantly between P30 and P60-70. Histochemical studies confirmed that activity of the mitochondrial respiratory enzymes cytochrome c oxidase (EC 1.9.3.1), succinate dehydrogenase (EC 1.3.99.1), and NADH-dehydrogenase (EC 1.6.99.3) increased monotonically during the developmental period in which planar growth of first-order dendrites was observed. The present results, in combination with results from previous studies, indicate that morphological and metabolic development fo the NST occurs concomitantly with morphological development of taste receptors and peripheral gustatory nerves.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Postnatal development of the rostral solitary nucleus in rat: dendritic morphology and mitochondrial enzyme activity. 246 1


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