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)

Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-nitrate reductase from Neurospora crassa was purified and found to be stimulated by certain amino acids, citrate, and ethylenediaminetetraacetic acid (EDTA). Stimulation by citrate and the amino acids was dependent upon the prior removal of EDTA from the enzyme preparations, since low quantities of EDTA resulted in maximal stimulation. Removal of EDTA from enzyme preparations by dialysis against Chelex-containing buffer resulted in a loss of nitrate reductase activity. Addition of alanine, arginine, glycine, glutamine, glutamate, histidine, tryptophan, and citrate restored and stimulated nitrate reductase activity from 29- to 46-fold. The amino acids tested altered the Km of NADPH-nitrate reductase for NADPH but did not significantly change that for nitrate. The Km of nitrate reductase for NADPH increased with increasing concentrations of histidine but decreased with increasing concentrations of glutamine. Amino acid modulation of NADPH-nitrate reductase activity is discussed in relation to the conservation of energy (NADPH) by Neurospora when nitrate is the nitrogen source.
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PMID:Regulation of the Neurospora crassa assimilatory nitrate reductase. 1 23

A positive, genetic selection against the activity of the nitrogen regulatory (NTR) system was used to isolate insertion mutations affecting nitrogen regulation in Klebsiella aerogenes. Two classes of mutation were obtained: those affecting the NTR system itself and leading to the loss of almost all nitrogen regulation, and those affecting the nac locus and leading to a loss of nitrogen regulation of a family of nitrogen-regulated enzymes. The set of these nac-dependent enzymes included histidase, glutamate dehydrogenase, glutamate synthase, proline oxidase, and urease. The enzymes shown to be nac independent included glutamine synthetase, asparaginase, tryptophan permease, nitrate reductase, the product of the nifLA operon, and perhaps nitrite reductase. The expression of the nac gene was itself highly nitrogen regulated, and this regulation was mediated by the NTR system. The loss of nitrogen regulation was found in each of the four insertion mutants studied, showing that loss of nitrogen regulation resulted from the absence of nac function rather than from an altered form of the nac gene product. Thus we propose two classes of nitrogen-regulated operons: in class I, the NTR system directly activates expression of the operon; in class II, the NTR system activates nac expression and the product(s) of the nac locus activates expression of the operon.
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PMID:Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes. 197 23

Carcinoma of the urinary bladder is the most common malignancy in Egyptians. At the National Cancer Institute in Cairo, it accounts for 27.6% of all cancers--38.5% of cancers in the male and 11.3% in the female. This very high frequency is attributed to underlying schistosomiasis. The infection can lead to malignancy through local tissue damage, mechanical irritation, bilharzial toxins or through secondary bacterial infection. Bacterial products include nitrate reductase capable of synthesizing nitrosoamines and beta glucuronidase enzymes, active at pH 7. Through liver involvement and dysfunction, tryptophan metabolism is disturbed, with the excretion of carcinogenic metabolites. Vitamin A deficiency is responsible for the squamous metaplasia and the high frequency of squamous cell carcinoma observed in the bladder. The characteristic clinico-pathological features of cancer of the urinary bladder are outlined, mainly the occurrence at a young age, the male predominance, especially farmers, and the high association with schistosomiasis. The tumors are often first seen in an advanced stage, arising from the posterior bladder wall and vault. The trigone is only affected in 8.5% of the cases. Histologically, squamous cell carcinomas of low grade are the most frequent cell type. Lymph node involvement is low in spite of the advanced stage of the tumor. Therefore, the results of radical surgery are encouraging. The results of a special study correlating the above parameters with the intensity of ova deposition are presented. Patients with heavy infection at a slightly earlier age but other tumor parameters the same are similar to those of egg-negative cases. This study indicates that other factors also play a role in the induction of tumors that are enhanced by the schistosomal infection. In Fayoum Province, schistosomiasis is decreasing while bladder cancer is increasing. Urine cytology as a screening tool is effective in detecting early bladder cancer. Studies are now in progress to detect tumor associated antigens in sera and urine of patients.
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PMID:Carcinoma of the urinary bladder associated with schistosomiasis in Egypt: the possible causal relationship. 314 81

Thirty-eight mutants unable to reduce nitrate were isolated from Escherichia coli and characterized biochemically and genetically. All of the mutants exhibited reduced or insignificant levels of formate dehydrogenase, nitrate reductase, or various combinations of these activities and cytochrome b(1) under conditions which resulted in the production of high levels of these activities by the wild-type parental strains. Most of the mutants reverted readily to wild type, and all mapped within a restricted region on the chromosome linked to the tryptophan genes. It was proposed that nitrate reduction in E. coli was catalyzed exclusively by an organized complex containing formate dehydrogenase, cytochrome b(1), and nitrate reductase.
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PMID:Nitrate reductase complex of Escherichia coli K-12: isolation and characterization of mutants unable to reduce nitrate. 488 9

The mob mutants of Escherichia coli are pleiotropically defective in molybdoenzyme activities because they are unable to catalyse the conversion of molybdopterin guanine dinucleotide, the active form of the molybdenum cofactor. The mob locus comprises two genes. The product of mobA, protein FA, has previously been purified to homogeneity and is able to restore molybdoenzyme activities following incubation with cell extracts of mob strains. The mobB gene, although not essential for the biosynthesis of active molybdoenzymes, encodes a protein which, sequence analysis strongly suggests, contains a nucleotide-binding site. We have overproduced the products of both the mobA and mobB genes in engineered E. coli strains and purified each to homogeneity. The preparation of protein FA (MobA) is simpler than that previously published and produces a much greater yield of active protein. The isolated MobB protein, which is dimeric in solution, acts in the presence of protein FA, to enhance the level of nitrate reductase activation achieved on incubation with mob cell extracts. Equilibrium dialysis experiments show that purified MobB binds 0.83 mol GTP/mol protein with a Kd of 2.0 microM. Isolated MobB also catalyses a low GTPase activity (turnover number of 3 x 10(-3) min-1) with a K(m) for GTP to GDP of 7.5 microM. Under the conditions tested, protein FA did not affect the GTP-binding or GTPase activity of MobB. Intrinsic (tryptophan) protein fluorescence measurements show that MobB also binds the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. These results are consistent with a model whereby MobB binds the guanine nucleotide which is attached to molybdopterin during the biosynthesis of the molybdenum cofactor.
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PMID:The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein. 921 27

The protective effects of L-cysteine, ascorbic acid, reduced glutathione, L-tryptophan, and sodium pyruvate against UV-B-induced damages were studied in the nitrogen-fixing cyanobacterium, Nostoc muscorum. When added to the culture suspension during UV-B treatment, these chemicals caused a significant protective effect on survival and growth of the organism. Sodium pyruvate conferred the strongest protection whereas the weakest effect was elicited by tryptophan. A 20 min exposure of a culture suspension to UV-B completely inactivated nitrogenase activity but the inactivation was strongly prevented by exogenous addition of ascorbic acid or reduced glutathione during UV-B exposure, and weakly prevented by pyruvate, cysteine and tryptophan. In vivo nitrate reductase activity was not completely lost even after 80 min of UV-B exposure, and addition of the test chemicals did not confer any significant protection to this enzyme. Whereas (14)CO(2) uptake was drastically inhibited (78% inhibition) by 30 min exposure to UV-B in the absence of any test chemical, about 76% activity remained when the UV-B exposure was given to cultures in the presence of ascorbic acid. These results suggest that the damaging effects of UV-B are substantially minimized by certain reducing agents, the protective effect being particularly strong on the O(2) sensitive enzyme, nitrogenase. Presence of these chemicals in their natural habitat or inside the cells of living organisms may partially protect/repair the damaging effects of UV-B radiation.
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PMID:Protective role of certain chemicals against UV-B-induced damage in the nitrogen-fixing cyanobacterium, Nostoc muscorum. 1274 56

A pot experiment was conducted to evaluate the effects of applying L-methionine (L-MET), L-phenylalanine (LPHE) and L-tryptophan (L-TRP) on the growth of Zea mays and its nutrient uptake, and to determine the optimal application rate of them. The results showed that L-MET, L-PHE and L-TRP could improve the shoot height, shoot and root dry weights, root activity, nitrate reductase and hydrogen peroxidase activities, and N, P, K and Zn uptake of corn. The optimal application rate of L-MET, L- PHE and L-TRP was 0.0185 - 0.185 mg x kg)(-1) soil, 0.2 mg x kg(-1) soil, and 0.03 - 0.3 mg x kg(-1) soil, respectively, and L-PHE and L-TRP were superior to L-MET.
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PMID:[Effects of applying L-methionine, L-phenylalanine and L-tryptophan on Zea mays growth and its nutrient uptake]. 1618 Jul 48

When Escherichia coli K-12 is grown anaerobically in medium containing tryptophan and sodium nitrate, it produces red compounds. The reaction requires functional genes for trytophanase (tnaA), a tryptophan permease (tnaB), and a nitrate reductase (narG), as well as a natural drop in the pH of the culture. Mass spectrometry revealed that the purified chromophores had mass/charge ratios that closely match those for indole red, indoxyl red, and an indole trimer. These compounds are known products of chemical reactions between indole and nitrous acid. They are derived from an initial reaction of 3-nitrosoindole with indole. Apparently, nitrite that is produced from the metabolic reduction of nitrate is converted in the acid medium to nitrous acid, which leads to the nitrosation of the indole that is generated by tryptophanase. An nfi (endonuclease V) mutant and a recA mutant were selectively killed during the period of chromophore production, and a uvrA strain displayed reduced growth. These effects depended on the addition of nitrate to the medium and on tryptophanase activity in the cells. Unexpectedly, the killing of a tnaA(+) nfi mutant was not accompanied by marked increases in mutation frequencies for several traits tested. The vulnerability of three DNA repair mutants indicates that a nitrosoindole or a derivative of a nitrosoindole produces lethal DNA damage.
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PMID:Production of 3-nitrosoindole derivatives by Escherichia coli during anaerobic growth. 1956 Nov 28