Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.7.1.2 (nitrate reductase)
3,861 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two commercially available micromethod multitest systems (API, Analytab Products, Inc., Minitek-Bioquest) were compared with conventional tests suggested by the Center for Disease Control for the identification of anaerobes. Anaerobiosis for the microsystems was achieved using GasPak system (BBL), A total of 175 anaerobes, including 158 clinical isolates and 17 reference strains, were used. Gram morphology, gas-liquid chromatography data, and biochemical reactions from the Center for Disease Control and Virginia Polytechnic Institute anaerobic manuals were used to identify the organisms. The Minitek system included a new anaerobe inoculum broth and two new disks, dextrose without nitrate and nitrate reductase disks. The percentage of correlation of 12 biochemicals using Minitek and 11 biochemicals using the API were compared with the Center for Disease Control reactions. The percentage of correlation of both positive and negative reactions with the API anaerobic strip ranged from 70.8 to 99.4% and with the Minitek from 97.1 to 100%. The microsystems were also evaluated as to the ease of use, adaptabilty to a clinical laboratory, time, and cost.
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PMID:Comparison of API and Minitek to Center for Disease Control methods for the biochemical characterization of anaerobes. 78 9

Spinach (Spinacia oleracea L.) leaf nitrate reductase (NADH:NR;NADH:nitrate oxidoreductase, EC 1.6.6.1) activity was found to rapidly change during light/dark transitions. The most rapid and dramatic changes were found in a form of NR which was sensitive to inhibition by millimolar concentrations of magnesium. This form of NR predominated in leaves in the dark, but was almost completely absent from leaves incubated in the light for only 30 min. When the leaves were returned to darkness, the NR rapidly became sensitive to Mg2+ inhibition. Modulation of the overall reaction involving NADH as electron donor was also found when reduced methyl viologen was the donor (MV:NR), indicating that electron transfer had been blocked, at least in part, at or near the terminal molybdenum cofactor site. Changes in activity appear to be the result of a covalent modification that affects sensitivity of NR to inhibition by magnesium, and our results suggest that protein phosphorylation may be involved. NR was phosphorylated in vivo after feeding excised leaves [32P]Pi. The NR subunit was labeled exclusively on seryl residues in both light and dark. Tryptic peptide mapping indicated three major 32P-labeled phosphopeptide (Pp) fragments. Labeling of two of the P-peptides (designated Pp1 and 3) was generally correlated with NR activity assayed in the presence of Mg2+. In vivo, partial dephosphorylation of these sites (and activation of NR assayed with Mg2+) occurred in response to light or feeding mannose in darkness. The light effect was blocked completely by feeding okadaic acid via the transpiration stream, indicating the involvement of type 1 and/or type 2A protein phosphatases in vivo. While more detailed analysis is required to establish a causal link between the phosphorylation status of NR and sensitivity to Mg2+ inhibition, the current results are highly suggestive of one. Thus, in addition to the molecular genetic mechanisms regulating this key enzyme of nitrate assimilation, NR activity may be controlled in leaves by phosphorylation/dephosphorylation of the enzyme protein resulting from metabolic changes taking place during light/dark transitions.
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PMID:Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation. 160 45

Escherichia coli cells grown anaerobically in the presence of nitrate reduce the nitrate as a terminal electron acceptor in place of molecular oxygen by an induced respiratory-type electron transferring system residing in the inner membrane structure. When oxygen is introduced to a suspension of nitrate-respiring cells, the oxygen is immediately reduced preferentially and the cellular uptake of nitrate ceases abruptly. In contrast, we found that the cells exhibited no oxygen control on uptake of chlorate, a competitive substrate analogue, indicating operation of an oxygen-sensitive transport system specific to nitrate. This was further evidenced by the fact that chlorate inhibition of reduction of nitrate was brought about only when the transport of both chlorate and nitrate was facilitated by the aid of carrier-type chlorate (or nitrate) ionophore. We demonstrated that oxygen inhibition on reduction of nitrate was abolished within the cells treated by octyl glucoside resulting in a removal of permeability barrier specific to nitrate. We conclude that the transient control by molecular oxygen is primarily due to the inhibition of nitrate transport into the cytoplasmic side. Since nitrate induces the nitrate-respiring system, the repression of the nitrate reductase operon by molecular oxygen is consistently interpreted on the basis of the "inducer exclusion mechanism."
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PMID:Molecular oxygen controls nitrate transport of Escherichia coli nitrate-respiring cells. 329 57

Four detergents (octyl glucoside, zwittergent, Triton X-100, and Nonidet P-40) were examined with regard to their efficiency in solubilizing and retaining the activity of the nitrate reductase of Bacillus stearothermophilus. At a concentration of between 0.4 and 0.6%, the non-ionic detergent octyl glucoside solubilized only 64% of the membrane proteins. However, about 100% of the nitrate reductase activity was recovered in the soluble fraction. In contrast, the zwitterionic detergent 3-(alkyldimethylammonio)-1-propanesulphonate (3-16) solubilized 100% of the membrane proteins, but only 77% of the nitrate reductase activity was recovered. Two other non-ionic detergents, Triton X-100 and Nonidet P-40 also solubilized 100% of the membrane proteins, but there was a dramatic increase in total enzyme activity following solubilization. The enzyme activity was not stable in any of the four detergents for more than 2 days. Nevertheless, octyl glucoside was preferred because of the additional advantage of ammonium sulphate fractionation.
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PMID:Detergent solubilization of the respiratory nitrate reductase of Bacillus stearothermophilus. 378 23

Biotyping of Haemophilus influenzae into five type and H. parainfluenzae into three types based on indole production, ornithine decarboxylase, and urease has been reported (M. Kilian, Acta Pathol. Microbiol. Scand. Sect. B 82:835--842, 1976). A commercially available test system designed for the 4-h identification of Enterobacteriaceae. Micro-ID, proved efficacious for the rapid biotyping of these two Haemophilus species. The nitrate reductase, indole production, ornithine decarboxylase, urease, and o-nitrophenyl-beta-D-galactopyranoside hydrolysis tests in Micro-ID correlated over 99% with conventional methodology. By utilizing the indole and o-nitrophenyl-beta-D-galactopyranoside tests it was possible, with 261 of 272 (96.1%) isolates, to distinguish H. influenzae from H. parainfluenzae. Cerebrospinal fluid isolates were over 90% H. influenzae biotype I, and conjunctival isolates were approximately 70% biotype II. Type b H. influenzae were predominantly biotypes I and II; these type b isolates were also overwhelmingly indole producers. Although over 90% of biotypes I and II have been reported to produce beta-lactamase, this was not confirmed by the small number of beta-lactamase producers encountered here. The 4-h Micro-ID should prove a useful mechanism, amenable to the routine clinical laboratory, for the further exploration of the association of Haemophilus with the site of isolation, antigenicity, and antibiotic resistance.
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PMID:Rapid biochemical characterization of Haemophilus species by using the micro-ID. 698 1

The aspartic proteinase (MPP) gene from the zygomycete fungus Mucor pusillus was introduced into an ascomycete fungus, Aspergillus oryzae, by protoplast transformation using the nitrate reductase (niaD) gene as the selective marker. Southern blot analysis indicated that the MPP gene was integrated into the resident niaD locus at a copy number of 1-2. MPP secreted by the recombinant A. oryzae was correctly processed but was more highly glycosylated than that produced in the original M. pusillus strain. Treatment with endo-beta-N-acetylglucosaminidase H and analysis of the carbohydrate composition of the secreted MPP revealed that the extra glycosylation of the MPP secreted by the recombinant A. oryzae was due to altered processing of mannose residues. The extra glycosylation of MPP affected its enzyme properties including its milk-clotting and proteolytic activities.
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PMID:Characterization of an aspartic proteinase of Mucor pusillus expressed in Aspergillus oryzae. 824 85

Phenotypic and phylogenetic studies were performed with two strains (OCh 317T and OCh 318; T = type strain) of aerobic chemoheterotrophic bacteriochlorophyll-containing bacteria isolated from water of a saline lake located on the west coast of Australia. Both strains were Gram-negative, short rods and were motile by means of polar flagella. Catalase, oxidase, nitrate reductase, phosphatase and urease were produced. The cells utilized D-glucose, citrate, glycolate, pyruvate and ethanol. Acids were produced from L-arabinose, D-fructose, D-galactose, D-glucose, D-ribose and D-xylose. The strains could grow in media containing 0.5-7.5% NaCl. Bacteriochlorophyll a was synthesized under aerobic conditions. The results of 16S rRNA gene sequence comparisons revealed that strain OCh 317T represented a new lineage in the alpha-3 group of the class Proteobacteria. Strains OCh 317T and OCh 318 were identified as strains of the same species because of their very similar phenotypic characteristics and their previously described high DNA-DNA homology. Therefore, it was concluded that the two strains should be assigned to a new genus and species, for which the name Rubrimonas cliftonensis is proposed. The type strain is OCh 317T (= JCM 10189T).
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PMID:Rubrimonas cliftonensis gen. nov., sp. nov., an aerobic bacteriochlorophyll-containing bacterium isolated from a saline lake. 1002 64

Phenotypic and phylogenetic studies were performed with two strains (OCh 239T and OCh 210T, T = type strain) of aerobic bacteriochlorophyll-containing bacteria isolated from the charophytes and the epiphytes on the stromatolites, respectively, of a saline lake located on the west coast of Australia. Both strains were chemoheterotrophic, Gram-negative and motile rods with subpolar flagella. Catalase and oxidase were produced. ONPG reaction was positive. Cells utilized D-glucose, acetate, butyrate, citrate, DL-lactate, DL-malate, pyruvate, succinate, L-aspartate and L-glutamate. Acids were produced from D-fructose and D-glucose. Bacteriochlorophyll a was synthesized under aerobic conditions. Strain OCh 239T had nitrate reductase and phosphatase. Acids were produced from L-arabinose, D-galactose, lactose, maltose, D-ribose and sucrose. The strain could grow in 0-20.0% (w/v) NaCl. Strain OCh 210T had urease. Hydrolysis of gelatin was positive. Acids were produced from D-xylose. The strain could grow in 0.5-20.0% (w/v) NaCl. The results of 16S rRNA sequence comparisons revealed that strains OCh 239T and OCh 210T formed a new cluster within the alpha-3 group of the alpha subclass of the class Proteobacteria. The similarity value of the 16S rRNA sequences between strains OCh 239T and OCh 210T was 95.8%. Therefore, it was concluded that these two strains should be placed in a new genus, Roseivivax gen. nov., as the new species Roseivivax halodurans sp. nov. and Roseivivax halotolerans sp. nov. The type species of the genus is Roseivivax halodurans. The type strains of Roseivivax halodurans and Roseivivax halotolerans are OCh 239T (= JCM 10272T) and OCh 210T (= JCM 10271T), respectively.
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PMID:Roseivivax halodurans gen. nov., sp. nov. and Roseivivax halotolerans sp. nov., aerobic bacteriochlorophyll-containing bacteria isolated from a saline lake. 1031 85

The Escherichia coli transcriptional regulatory complex FlhD/FlhC, initially identified as a flagella-specific activator, is a global regulator involved in many cellular processes. Using gene arrays, lacZ gene fusions and enzyme assays, eight new targets of FlhD/FlhC were recognized. These are the transporter for galactose (MglBAC), the rod-shape determination proteins (MreBCD), malate dehydrogenase, and several enzymes involved in anaerobic respiration (glycerol 3-phosphate dehydrogenase, GlpABC; periplasmic nitrate reductase, NapFAGHBC; nitrite reductase, NrfABCDEFG; dimethyl sulfoxide reductase, DmsABC; and the modulator for hydrogenases, HydNHypF).
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PMID:FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions. 1128 52

Nitrate reductase (NR) (EC 1.6.6.1) activity and NR activation state, i.e. activity in the presence of Mg(2+) relative to activity in the absence of Mg(2+), in cucumber (Cucumis sativus) leaves increased in the light and decreased in the dark. In contrast to leaves, NR activation state in the roots did not show light/dark-dependent changes. Root NR was activated by anoxia or by addition of uncoupler (CCCP) or mannose. These treatments decreased ATP levels in root tissue. On the contrary, high oxygen supply promoted some NR inactivation. When an extract from anoxic roots was preincubated with ATP, NR was gradually inactivated. Subsequent addition of 5'-AMP resulted in a remarkable reactivation of the enzyme. NR extracted from hyperoxygenated roots was activated by preincubation with 5'-AMP, and the process was reversed by ATP. These results suggest the participation of adenine nucleotides on the in vivo modulation of NR activity in cucumber roots. NR was activated in vivo by cellular acidification and inactivated by alkalinisation. The acid-induced activation of NR was greatly prevented by okadaic acid, a protein phosphatase inhibitor. Our data indicate that, as in barley roots, anoxia, uncouplers, and mannose feeding activate cucumber root NR, at least partly, by enhancing NR dephosphorylation via a decrease in the internal level of ATP and a concomitant cellular acidification.
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PMID:Modulation of nitrate reductase activity in cucumber (Cucumis sativus) roots. 1144 53


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