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

Streptococcus thermophilus STH450 had a very high oxygen uptake. This strain was then compared with aerobic metabolism to S. thermophilus ATCC 19258, a reference strain for aerobic metabolism. Molecular oxygen, which was absorbed by S. thermophilus STH450 during aerobic glycolytic metabolism, was involved in the oxidation of NADH by the catalytic activity of NADH oxidase. The portion of pyruvate that corresponded to the oxidized NADH was committed to form alpha-acetolactate, acetoin, and diacetyl. Both strains were deficient in peroxidase and pyruvate oxidase activities; therefore, NADH oxidase was probably the terminal oxidase in aerobic glycolytic metabolism. Oxygen uptake and NADH oxidase activities were significantly higher in S. thermophilus STH450 than in S. thermophilus ATCC 19258. alpha-Acetolactate, acetoin, and diacetyl also accumulated during aerobic glycolytic metabolism of S. thermophilus STH450. However, when both strains were grown in the presence of pyruvate, these metabolites were equivalent. Hence, less oxygen might be needed for pyruvate metabolism.
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PMID:Oxygen uptake activity and aerobic metabolism of Streptococcus thermophilus STH450. 358 99

Addition of vanadate, stimulated oxidation of NADH by rat liver microsomes. The products were NAD+ and H2O2. High rates of this reaction were obtained in the presence of phosphate buffer and at low pH values. The yellow-orange colored polymeric form of vanadate appears to be the active species and both ortho- and meta-vanadate gave poor activities even at mM concentrations. The activity as measured by oxygen uptake was inhibited by cyanide, EDTA, mannitol, histidine, ascorbate, noradrenaline, adriamycin, cytochrome c, Mn2+, superoxide dismutase, horseradish peroxidase and catalase. Mitochondrial outer membranes possess a similar activity of vanadate-stimulated NADH oxidation. But addition of mitochondria and some of its derivative particles abolished the microsomal activity. In the absence of oxygen, disappearance of NADH measured by decrease in absorbance at 340 nm continued at nearly the same rate since vanadate served as an electron acceptor in the microsomal system. Addition of excess catalase or SOD abolished the oxygen uptake while retaining significant rates of NADH disappearance indicating that the two activities are delinked. A mechanism is proposed wherein oxygen receives the first electron from NAD radical generated by oxidation of NADH by phosphovanadate and the consequent reduced species of vanadate (Viv) gives the second electron to superoxide to reduce it H2O2. This is applicable to all membranes whereas microsomes have the additional capability of reducing vanadate.
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PMID:Vanadate-stimulated NADH oxidation in microsomes. 365 Jun 94

The transient state kinetics of the oxidation of reduced nicotinamide adenine dinucleotide (NADH) by horseradish peroxidase compound I and II (HRP-I and HRP-II) was investigated as a function of pH at 25.0 degrees C in aqueous solutions of ionic strength 0.11 using both a stopped-flow apparatus and a conventional spectrophotometer. In agreement with studies using many other substrates, the pH dependence of the HRP-I-NADH reaction can be explained in terms of a single ionization of pKa = 4.7 +/- 0.5 at the active site of HRP-I. Contrary to studies with other substrates, the pH dependence of the HRP-II-NADH reaction can be interpreted in terms of a single ionization with pKa of 4.2 +/- 1.4 at the active site of HRP-II. An apparent reversibility of the HRP-II-NADH reaction was observed. Over the pH range of 4-10 the rate constant for the reaction of HRP-I with NADH varied from 2.6 X 10(5) to 5.6 X 10(2) M-1 s-1 and of HRP-II with NADH varied from 4.4 X 10(4) to 4.1 M-1 s-1. These rate constants must be taken into consideration to explain quantitatively the oxidase reaction of horseradish peroxidase with NADH.
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PMID:Kinetics of the oxidation of reduced nicotinamide adenine dinucleotide by horseradish peroxidase compounds I and II. 371 6

The effects of carbon disulfide (CS2) on the liver microsomal drug-metabolizing enzyme system and other enzyme activities were studied 1 hr after the oral administration of 3-300 mg/kg of CS2 in mice. Considerable decreases in drug-metabolizing enzyme activities (such as hydroxylation of aniline, O-dealkylation of p-nitroanisole, 7-ethoxycoumarin and 7-ethoxyresorufin, and N-demethylation of N,N-dimethylaniline), NADPH-cytochrome P-450 reductase (but not NADPH-cytochrome c reductase), and P-450-associated peroxidase activities were already observed at 3 and 30 mg/kg of CS2, dose dependently. At the same dosage levels, the magnitudes of microsomal spectral changes induced by aniline and nicotinamide (type 2 substrates), but not those induced by hexobarbital and SKF-525A (type 1 substrates), were also reduced to a considerable extent. The degrees of these alterations were all greater than that of the measurable loss of P-450 content, i.e. the loss of functional activity of P-450 was much greater than simply expected from the apparent decrease in the hemoprotein content. Cytochrome b5 content and NADH-ferricyanide reductase activity were unchanged at 30 and 300 mg/kg of CS2, although NADH-cytochrome c reductase activity was increased at the latter dose. The following enzyme activities did not change significantly at up to 300 mg/kg of CS2: flavin-containing monooxygenase, UDP-glucuronyl transferase, glucose-6-phosphatase and heme oxygenase in microsomes, and glutathione S-transferases in the soluble fraction. Microsomal conjugated diene levels and liver glutathione content were also unchanged. These observations support the theory that P-450 is a sensitive and selective site for CS2 action, where CS2 itself is bioactivated. It was also shown that the loss of P-450 was reversible after a single, or repeated, administration of CS2.
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PMID:Early, selective and reversible suppression of cytochrome P-450-dependent monooxygenase of liver microsomes following the administration of low doses of carbon disulfide in mice. 377 18

The parameters of enzyme electrodes based on organic metals are presented. Cytochrome b2 (E.C. 1.1.2.3), glucose oxidase (E.C. 1.1.3.4), xanthine oxidase (E.C. 1.2.3.2) and peroxidase (E.C. 1.11.1.7) were used in electrodes sensitive to L-lactate, glucose, hypoxanthine and hydrogen peroxide. Electrocatalytic oxidation of NADH on organic metals and ethanol and acetaldehyde sensitive electrodes containing alcohol dehydrogenase (E.C. 1.1.1.1) were studied. Biocatalytic charge accumulation, the mechanism of electron exchange between the enzyme active centres and organic metals, and the future application of organic metals are discussed.
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PMID:Enzyme electrodes based on organic metals. 379 Jan 76

The manganese peroxidase (MnP), from the lignin-degrading fungus Phanerochaete chrysosporium, an H2O2-dependent heme enzyme, oxidizes a variety of organic compounds but only in the presence of Mn(II). The homogeneous enzyme rapidly oxidizes Mn(II) to Mn(III) with a pH optimum of 5.0; the latter was detected by the characteristic spectrum of its lactate complex. In the presence of H2O2 the enzyme oxidizes Mn(II) significantly faster than it oxidizes all other substrates. Addition of 1 M equivalent of H2O2 to the native enzyme in 20 mM Na-succinate, pH 4.5, yields MnP compound II, characterized by a Soret maximum at 416 nm. Subsequent addition of 1 M equivalent of Mn(II) to the compound II form of the enzyme results in its rapid reduction to the native Fe3+ species. Mn(III)-lactate oxidizes all of the compounds which are oxidized by the enzymatic system. The relative rates of oxidation of various substrates by the enzymatic and chemical systems are similar. In addition, when separated from the polymeric dye Poly B by a semipermeable membrane, the enzyme in the presence of Mn(II)-lactate and H2O2 oxidizes the substrate. All of these results indicate that the enzyme oxidizes Mn(II) to Mn(III) and that the Mn(III) complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds. In the absence of exogenous H2O2, the Mn-peroxidase oxidized NADH to NAD+, generating H2O2 in the process. The H2O2 generated by the oxidation of NADH could be utilized by the enzyme to oxidize a variety of other substrates.
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PMID:Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium. 380 Mar 95

Incubation of cellulose, sodium carboxylcellulose, pectin, polygalacturonic acid, xylan and arabinogalactan with hydrogen peroxide (0.1-10 mM) resulted in rapid breakdown of the polysaccharides when measured by a reduction of solution viscosity or an increase in reducing groups. When the reaction mixtures were precipitated with ethanol or fractionated on G-25-300 Sephadex, low molecular weight reducing groups increased with incubation time indicating that polymer cleavage was occurring and not simply polymer modification. Oxidation was most rapid at pH 6.5 or 7.5, although secondary optima between pH 3.5 and 5.5 were also observed, depending on the polysaccharide. Purified cell walls isolated from various organs of tomato, cucumber and soybean were similarly degraded and the ethanol-soluble reaction products were partially characterized. The data support the hypothesis that hydrogen peroxide generated by peroxidase from NADH may play a role during cell wall breakdown in plants.
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PMID:Oxidation of cell wall polysaccharides by hydrogen peroxide: a potential mechanism for cell wall breakdown in plants. 380 Sep 97

We describe methods for automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid. Phospholipase C (EC 3.1.4.3) and sphingomyelin phosphodiesterase (EC 3.1.4.12) are reacted with lecithin and sphingomyelin, respectively, to liberate phosphocholine. Phosphocholine is then reacted with alkaline phosphatase, choline oxidase, peroxidase, and 4-aminoantipyrine to form a colored complex, for which the absorbance at 500 nm is measured with a centrifugal analyzer. Phosphatidylglycerol is hydrolyzed by phospholipase D (EC 3.1.4.4) to form glycerol, which is subsequently reacted with ATP and NAD+ in the presence of glycerol kinase and glycerol-3-phosphate dehydrogenase to yield NADH. The absorbance of the NADH formed is measured at 340 nm. These methods provide a simple, rapid, and accurate alternative to thin-layer chromatography for determination of phospholipids in amniotic fluid for assessment of fetal lung maturity.
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PMID:Automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid. 380 1

A novel procedure for a simultaneous demonstration of particular enteric nerve cell types and peptidergic nerve fibres has been developed by combining the histochemical reaction for NADH-dependent dehydrogenase and the unlabelled antibody peroxidase-antiperoxidase (PAP) method described by Sternberger. Whole-mount spreads were successively incubated in a NADH: nitroblue tetrazolium solution, fixed with a picric acid/formaldehyde mixture, dehydrated, cleared and rehydrated before processing for immunocytochemical localization of the neuropeptide by the PAP method. The nerve cells appear heavily stained by deposits of dark blue formazan, whereas the peptide-containing nerves appear bright brown. In the myenteric and submucous plexuses of the porcine small intestine the devised method allows an appropriate identification of Dogiel's type I, type II and type III neurons surrounded by varicose enkephalin-like immunoreactive fibre baskets with button-like twigs to the very surface of the ganglionic cells, suggestive of synaptic connections.
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PMID:NADH-dehydrogenase reaction in combination with immunoperoxidase (PAP) staining for light microscopic observation on the interneuronal relations of the enteric nervous system of the pig. 390 47

The selective interaction of low concentrations of azole derivatives and other nitrogen heterocycles with cytochrome P-450 may be at the origin of the inhibition of ergosterol biosynthesis. From the depletion of ergosterol and the concomitant accumulation of 14 alpha-methylsterols, alterations in membrane functions, the synthesis and activity of membrane-bound enzymes, mitochondrial activities, and an uncoordinated activation of chitin synthase may result. Since chitin synthesis is more important in the hyphal form than in the budding form of C. albicans, the uncoordinated activation of chitin synthesis may be more trouble for the hyphal growth than for yeast budding. The assumption is made that from this difference the greater sensitivity of hyphal growth to azole antifungal agents may originate. It is also assumed that the higher degree of lipid unsaturation may be related to an inhibition of ergosterol biosynthesis. The inhibition of fatty acid desaturation and elongation induced by higher doses of miconazole and ketoconazole and the longer contact times might be related to interference with membrane fluidity, or it might due to chelation of the iron used in the oxidation reduction sequence during desaturation. The decreased availability of ergosterol and the accumulation of 14 alpha-methylsterols also may provide the environment needed to inactivate membrane-bound enzymes; e.g., cytochrome c peroxidase. However, it is still too speculative to correlate effects on membrane components with miconazole-induced changes in properties of all oxidases; e.g., the NADH-dependent, cyanide-insensitive oxidase. The accumulation of toxic concentrations of hydrogen peroxide, resulting from an increased NADH-oxidase activity and disappearance of the peroxidase and catalase activity, may contribute to the degeneration of subcellular structures. The complete disappearance of catalase observed at concentrations of miconazole greater than or equal to 10(-5) M may originate from direct effects on the cell. At these high concentrations reached only by topical application, direct membrane damage resulting from interaction of miconazole with lipids was observed. These direct interactions result in an inhibition of membrane-bound enzyme and mitochondrial activities and in leakage of intracellular components. The direct interactions were much less pronounced in cells treated with ketoconazole. This correlates with the smaller area occupied in the membrane per ketoconazole molecule (30 A2), compared with that occupied in the membrane per miconazole molecule (90 A2).(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Biochemical targets for antifungal azole derivatives: hypothesis on the mode of action. 391 72


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