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)

The new API 20C yeast identification system together with appropriate microscopic morphology determinations achieved a 97% correlation with a rapid conventional method. Whereas a group composed of Candida, Torulopsis, Saccharomyces, and Rhodotorula was identified with ease (98% overall correlation), a second group, containing Cryptococcus, Trichosporon, and Geotrichum species, appeared to give the system the most difficulty (90% correlation). Within this group particular difficulty was encountered in identifying varieties of Cryptococcus albidus, C. terreus, C. laurentii, Trichosporon beigelli, and Geotrichum spp. as to species. The API 20C system should be incubated the full 72 h prescribed by the manufacturer. However, when used in conjunction with appropriate morphological tests, presumptive identifications of some Candida and Torulopsis species may be made at 24 to 48 h. To facilitate identifications of the more difficult group of yeasts, ancillary tests for determining nitrate reductase, urease, and phenol oxidase activities should be considered as additions to the strip. Incorporating the phenol oxidase test would be especially important for identification of Cryptococcus neoformans, a yeast which should be identified as quickly and as accurately as possible. The API 20C system with computer assistance has proved to be an easy-to-inoculate, versatile, and fairly rapid method of yeast identification, giving results comparable to those obtained by conventional methodologies.
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PMID:Evaluation of the new API 20C strip for yeast identification against a conventional method. 38 21

Molybdenum cofactor activity was found in the soluble fraction of cell-free extracts of Escherichia coli grown aerobically in media supplemented with molybdate. Cofactor was detected by its ability to complement the nitrate reductase-deficient mutant of Neurospora crossa, nit-1, resulting in the vitro formation of nitrate reductase activity. Acid treatment of E. coli extracts was not required for release of cofactor activity. Cofactor was able to diffuse through a membrane of nominal 2,000-molecular-weight cutoff and was insensitive to trypsin. The cofactor was associated with a carrier molecule (approximately 40,000 daltons) during gel filtration and sucrose gradient centrifugation, but was easily removed from the carrier by dialysis. The carrier molecule protected the cofactor from inactivation by heat or oxygen. E. coli grown in molybdenum-free media, without and with tungsten, synthesized a metal-free "empty" cofactor and its tungsten analog, respectively, both of which were subsequently activated by the addition of molybdate. Empty and tungsten-containing cofactor complemented the nitrate reductase subunits in the nit-1 extract, forming inactive, but intact, 7.9S nitrate reductase. Addition of molybdate to the enzyme complemented in this manner restored nitrate reductase activity.
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PMID:Characterization of molybdenum cofactor from Escherichia coli. 38 15

We have used the penicillin selection method of Autissier & Kepes [(1972) Biochimie 54, 93--101] to study the segregation of membrane-bound respiratory nitrate reductase (EC 1.9.6.1) in Escherichia coli for the three generations after cessation of nitrate reductase synthesis caused by withdrawal of nitrate from the growth medium. We also included a physical separation procedure that permitted direct assay for nitrate reductase activity among all fractions produced by the penicillin selection method. We conclude that the segregation of nitrate reductase after cell division is dispersive, and not semi-conservative as proposed by Autissier & Kepes (1972).
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PMID:Synthesis of cytoplasmic membrane during growth and division of Escherichia coli. Dispersive behaviour of respiratory nitrate reductase. 39 53

The maize root has two main proteinase and carboxypeptidase components. Proteinase I and carboxypeptidase I, which predominate in older plants, appear to have a serine group at their active sites and have been estimated to have molecular weights of approximately 54000 and 77000 respectively. Proteinase I, which has been purified up to 500-fold, degrades haemoglobin and azocasein with maximum activity at pH 4 and 9--10 respectively, while on maize root protein it gives most hydrolysis in the neutral pH range. The main portion of the nitrate-reductase-inactivating activity in the maize root extract is due to proteinase I. Carboxypeptidase I, like several other plant carboxypeptidases such as carboxypeptidase C which have now (IUB Recommendations 1978) been classified as serine carboxypeptidases (EC 3.4.16.1), has maximum activity around pH 5 and has esterase activity. A second group of proteases, proteinase II and carboxypeptidase II, separated from the above on carboxymethyl-cellulose, were shown to have different molecular weight properties and be equally sensitive to serine and thiol group inhibitors. Proteinase II degrades haemoglobin, but not azocasein and does not mediate nitrate reductase inactivation. Associated with this second group of proteases was a macromolecular component which inactivated nitrate reductase but, unlike the action of proteinase I, was not inhibited by phenylmethylsulphonyl fluoride or casein. It was inhibited by metal chelating agents which were without effect on nitrate reductase inactivation due to proteinase I.
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PMID:Isolation and characterisation of peptide hydrolases from the maize root. 39 8

We have designed a new medium for the differentiation of mutants of Salmonella typhimurium defective in the ability to reduce nitrate with formate, and have characterized 24 formate dehydrogenase (FDH) mutants isolated on this medium. The mutants were assayed for the ability to use formate to reduce benzyl viologen and phenazine methosulfate, and were mapped by means of conjugation and P22-mediated transduction. Mutants lacking the ability to reduce either dye were found to map at three distinct sites: at a site co-transducible with xyl (presumably fdhA), at a site or sites between 13U and 33U, but not co-transducible with aroA, bio, purB, pyrC, or pyrD (near, but not identical with fdhB), and at asite 10-20% co-transducible with pyrE, for which we suggest the designation fdhC. Six mutant isolates reduced benzyl viologen, but not phenazine methosulfate. They retained the ability to produce nitrite during growth with nitrate. They mapped between 83U and 89U, but no co-transduction was found with metE, glnA, metB, or argH. The combined biochemical and genetic data suggest the existence of a gene in this area which is essential for the reduction of nitrate with formate, but not for formate hydrogenlyase activity or for nitrate reductase activity.
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PMID:Formate dehydrogenase mutants of Salmonella typhimurium: a new medium for their isolation and new mutant classes. 39 18

In E. coli K12 (F'nif+Kp) hybrids, electron-transport-dependent phosphorylation is not necessary for anaerobic nitrogen fixation, and substrate level phosphorylation can provide sufficient ATP from glucose for nitrogenase activity. The fumarate-reduction system, however, is essential in these hybrids for the transfer of electrons to nitrogenase. This system is probably also involved in maintaining the membrane in the energized state, thereby allowing nitrogen fixation to occur. The nitrate-reduction system, which can energize the membrane like the fumarate-reduction system, is not necessary for nitrogenase activity in the E. coli K12(F'nif+Kp) hybrids. However, two nitrate reductase genes, chlA, and chlB, are essential for inhibition of nitrogen fixation by nitrate. Moreover, nitrate inhibits nitrogenase activity and this inhibition is most probably effected through a regulator factor coded by chlA and chlB.
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PMID:Pathways of energy metabolism required for phenotypic expression of nif+Kp genes in Escherichia coli. 39 94

In animals the terminal step in the pathway for degradation of sulphur-containing amino acids is the oxidation of sulphite to sulphate. This reaction is catalysed by the enzyme sulphite oxidase. The enzyme contains molybdenum and a cytochrome b5 type haem, is localized in the mitochondrial intermembrane space and transfers electrons from sulphite to cytochrome c on the inner membrane. The sulphite oxidase protein has a molecular weight of 110 000 (chicken) to 122 000 (human) and exists as a dimer of identical subunits. The haem and molybdenum cofactors are present on separate domains of the molecule. The structure of the molydbenum cofactor has not been worked out in detail, but this cofactor is known to be present in many other molybdoenzymes including xanthine oxidase and nitrate reductase. Three cases of genetic sulphite oxidase deficiency in humans have been reported. The three affected children displayed mental retardation, neurological abnormalities and dislocated ocular lenses. The biochemical basis for lack of enzyme activity in each case has been studied. All three have been shown to lack the sulphite oxidase protein, but in one case this appears to be secondary to a defect in synthesis of the molybdenum cofactor. Sulphite oxidase deficiency has been produced in the rat by administration of high levels of tungsten. Sulphite oxidase-deficient animals are particularly susceptible to the toxic effects of sulphite and atmospheric sulphur dioxide.
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PMID:The oxidation of sulphite in animals systems. 39 60

Spontaneous chlorate-resistant (Clr) mutants of three classes were isolated from Nostoc muscorum under three different selective conditions. A Clr-N2 class of mutants lacked nitrate reductase and showed nitrate inhibition of nitrogen fixation. A Clr-NO3 group of het+ nif- mutants formed heterocysts, but lacked nitrogen fixation and active nitrogenase enzyme. The Clr-NO2 class included those mutants deficient in both active nitrogenase and nitrate reductase, as they were unable to grow at the expense of molecular nitrogen or with nitrate nitrogen. The results suggest a common genetic determinant of active nitrogenase and nitrate reductase in the blue-green alga N. muscorum.
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PMID:Isolation and characterization of chlorate-resistant mutants of the blue-green alga Nosoc muscorum. 40 80

In two out of three pleiotropic mutants of Rhizobium meliloti, defective in nitrate reductase induced by amino acid utilization in vegetative bacteria and in symbiotic nitrogen fixation, nitrogenase activity could be restored completely by purines and partially by the amino acids L-glutamate, L-aspartate, L-glutamine, and L-asparagine. The compounds restoring effectiveness in nitrogen fixation did not restore nitrate reductase activity in vegetative bacteria. The restoration of effectiveness supports our earlier conclusion that the mutation is not in the structural gene for a suggested common subunit of nitrogenase and nitrate reductase.
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PMID:Phenotypic reversion of nitrogenase in pleiotropic mutants of Rhizobium meliloti. 45 48

The cytoplasmic nitrate reductase in heme mutant H-14 of Staphylococcus aureus was partially purified by steps which included ammonium sulfate fractionation and chromatography on Bio-Gel A 1.5m and ion-exchange columns. The active fractions from the ion-exchange columns showed two forms of the enzyme upon electrophoresis in nondenaturing gels of polyacrylamide; these corresponded to proteins of R(f) 0.16 and 0.28. Each form contained a predominant polypeptide of molecular weight 140,000, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The R(f) 0.16 form contained another major polypeptide of molecular weight 57,000, but the R(f) 0.28 form contained several other polypeptides. The sedimentation properties of the enzyme were examined after partial purification on Bio-Gel A 1.5m. In sucrose gradients containing Triton X-100 the enzyme sedimented as a homogeneous peak with an estimated molecular weight of 225,000; without detergent a heterogeneous profile was observed of molecular weight greater than 250,000. Treatment of the enzyme with trypsin increased the specific activity, and the enzyme sedimented as a homogeneous peak in sucrose gradients without Triton X-100, with an estimated molecular weight of 202,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that trypsin treatment converted the polypeptide of molecular weight 140,000 to a polypeptide of molecular weight 112,000. We conclude that the cytoplasmic nitrate reductase of S. aureus has a large subunit of molecular weight 140,000, which can be modified by trypsin to a polypeptide of molecular weight 112,000 without loss of catalytic activity.
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PMID:Partial purification and some properties of the Staphylococcus aureus cytoplasmic nitrate reductase. 45 98


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