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)

Molybdenum cofactor (mocofactor) is extracted efficiently, free of impurities and in high concentrations, by acid treatment of xanthine oxidase and subsequent incubation of the precipitate with phosphate buffer containing EDTA, molybdate and oxygen. It is suggested that cofactor is bound to the enzyme via hydrophobic forces as well as via an oxygen-sensitive mechanism. Upon extraction, the capability to complement the apo nitrate reductase of Neurospora crassa nit-1 can be conserved only in the total absence of oxygen. Cysteine and glutathione were shown to protect efficiently free mocofactor from oxidation. Two species of active mocofactor, probably a molybdoform and a demolybdoform, could be separated by means of reversed-phase HPLC with a mobile phase of 5 mM sodium citrate at a pH of 6.5. The mode of interaction between either of these species with thiol reagents is discussed.
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PMID:Extraction and purification of molybdenum cofactor from milk xanthine oxidase. 369 96

The napEDABC locus coding for the periplasmic nitrate reductase of Thiosphaera pantotropha has been cloned and sequenced. The large and small subunits of the enzyme are coded by napA and napB. The sequence of NapA indicates that this protein binds the GMP-conjugated form of the molybdopterin cofactor. Cysteine-181 is proposed to ligate the molybdenum atom. It is inferred that the active site of the periplasmic nitrate reductase is structurally related to those of the molybdenum-dependent formate dehydrogenases and bacterial assimilatory nitrate reductases, but is distinct from that of the membrane-bound respiratory nitrate reductases. A four-cysteine motif at the N-terminus of NapA binds a [4Fe-4S] cluster. The DNA- and protein-derived primary sequence of NapB confirm that this protein is a dihaem c-type cytochrome and, together with spectroscopic data, indicate that both NapB haems have bis-histidine ligation. napC is predicted to code for a membrane-anchored tetrahaem c-type cytochrome that shows sequence similarity to the NirT cytochrome c family. NapC may be the direct electron donor to the NapAB complex. napD is predicted to encode a soluble cytoplasmic protein and napE a monotopic integral membrane protein, napDABC genes can be discerned at the aeg-46.5 locus of Escherichia coli K-12, suggesting that this operon encodes a periplasmic nitrate reductase system, while napD and napC are identified adjacent to the napAB genes of Alcaligenes eutrophus H16.
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PMID:The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. 763 19

Cysteine synthesis from sulfide and O-acetyl-L-serine (OAS) is a reaction interconnecting sulfate, nitrogen, and carbon assimilation. Using Lemna minor, we analyzed the effects of omission of CO(2) from the atmosphere and simultaneous application of alternative carbon sources on adenosine 5'-phosphosulfate reductase (APR) and nitrate reductase (NR), the key enzymes of sulfate and nitrate assimilation, respectively. Incubation in air without CO(2) led to severe decrease in APR and NR activities and mRNA levels, but ribulose-1,5-bisphosphate carboxylase/oxygenase was not considerably affected. Simultaneous addition of sucrose (Suc) prevented the reduction in enzyme activities, but not in mRNA levels. OAS, a known regulator of sulfate assimilation, could also attenuate the effect of missing CO(2) on APR, but did not affect NR. When the plants were subjected to normal air after a 24-h pretreatment in air without CO(2), APR and NR activities and mRNA levels recovered within the next 24 h. The addition of Suc and glucose in air without CO(2) also recovered both enzyme activities, with OAS again influenced only APR. (35)SO(4)(2-) feeding showed that treatment in air without CO(2) severely inhibited sulfate uptake and the flux through sulfate assimilation. After a resupply of normal air or the addition of Suc, incorporation of (35)S into proteins and glutathione greatly increased. OAS treatment resulted in high labeling of cysteine; the incorporation of (35)S in proteins and glutathione was much less increased compared with treatment with normal air or Suc. These results corroborate the tight interconnection of sulfate, nitrate, and carbon assimilation.
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PMID:Interaction of sulfate assimilation with carbon and nitrogen metabolism in Lemna minor. 1242 5

Pokkah boeng disease (PBD) is a foliar disease causing severe losses in sugarcane crop production. Research into resistance mechanisms against the causal agent, Fusarium verticillioides, is particularly important for farmers and researchers. This work based on the comprehensive analysis of metabolic, proteomic, and bioinformatics data on nitrogen (N) metabolism, which revealed that this biosynthetic reactions was closely related to resistance mechanisms in the sugarcane- F. verticillioides interaction. Our results suggested that pathogen infection reduced the suppression of nitrate reductase (NR) activity, reducing ammonium nitrogen (NH4+-N) and nitrate nitrogen (NO3--N) assimilation, which reduces glutamine synthetase (GS), glutamate synthetase (GOGAT) activity and polynucleotide synthesis and promotes RNA degradation, resulting in a decrease in ribosome levels and protein synthesis. Cysteine was found to be associated with the symptoms of PBD, while alanine, lysine, proline, and glutamic acid were found to be involved in protective and regulatory mechanisms as well. Additionally, glutamate played an important role in sugarcane defense against pathogens through the biosynthesis of proline and polyamines. Cyanamide, glutamate, proline, tyrosine, and arachidonic acid metabolism actively participate in resistance and response to stress. C5XPZ6 and C5XCA6 were considered to be critical proteins and key effectors according to this study. In conclusion, we have identified potential proteins and pathways involved in sugarcane resistance to F. verticillioides, revealing new findings that may be useful in the design of future diagnostics or sugarcane protection strategies and providing new insights into the molecular mechanisms of sugarcane-pathogen interactions.
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PMID:Metabolic and proteomic analysis of nitrogen metabolism mechanisms involved in the sugarcane - Fusarium verticillioides interaction. 3259 20