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 immunoaffinity chromatography of total membrane proteins from Escherichia coli helped determine the specificity of the monoclonal antibody 3A6 that was obtained upon immunization of mice with nicotinamide nucleotide transhydrogenase preparations and reacted with an unknown E. coli antigen. Proteins with apparent molecular masses of 150, 45, and 20 kDa were isolated and identified by N-terminal sequencing as the subunits of nitrate reductase. This conclusion was confirmed by immunoblotting with the 3A6 antibody of the proteins from the E. coli cells grown upon induction of nitrate reductase. It was shown that the 3A6 antibody specifically recognizes the alpha subunit of nitrate reductase, and the formation of the enzyme-antibody complex does not result in a loss of the enzyme catalytic activity.
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PMID:[Identification of Escherichia coli nitrate reductase as an antigen for a monoclonal antibody with previously unknown specificity]. 1104 Sep 97

Nitrate reductase (NR; EC 1.6.1.1-3) can be controlled at both transcriptional and posttranscriptional levels. Here we describe stability of NR mRNA as a mechanism of control. The NR gene in Chlorella vulgaris (Warburg strain) transcribes a stable mRNA and an unstable mRNA. In-vitro-synthesized transcripts representing these mRNAs show the same stability characteristics. The unstable mRNA is 30 nucleotides longer at the 5'-UTR compared to the stable mRNA. Using an RNA-folding program the 5'-UTR of the longer unstable RNA showed a more extensive stem-loop structure compared to the more linear form of the shorter stable mRNA. Transcripts representing RNAs with intermediate 5'-UTRs folded similarly to the long form and were unstable, or similarly to the short form and were more stable. Thus the secondary structure of the 5'-UTR of NR mRNA is important in the stability of NR transcripts in Chlorella and allows the cell to respond to changes in nitrogen source in an energy-efficient manner.
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PMID:The stability of the Chlorella nitrate reductase mRNA is determined by the secondary structure of the 5'-UTR: implications for posttranscriptional regulation of nitrate reductase. 1185 53

To investigate the role of stress in nitrogen management in plants, the effect of pathogen attack, elicitors, and phytohormone application on the expression of the two senescence-related markers GS1 (cytosolic glutamine synthetase EC 6.3.1.2) and GDH (glutamate dehydrogenase, EC 1.4.1.2) involved in nitrogen mobilization in senescing leaves of tobacco (Nicotiana tabacum L.) plants, was studied. The expression of genes involved in primary nitrogen assimilation such as GS2 (chloroplastic glutamine synthetase) and Nia (nitrate reductase, EC 1.6.1.1) was also analysed. The Glubas gene, coding a beta-1,3-glucanase, was used as a plant-defence gene control. As during natural senescence, the expression of GS2 and Nia was repressed under almost all stress conditions. By contrast, GS1 and GDH mRNA accumulation was increased. However, GS1 and GDH showed differential patterns of expression depending on the stress applied. The expression of GS1 appeared more selective than GDH. Results indicate that the GDH and GS1 genes involved in leaf senescence are also a component of the plant defence response during plant-pathogen interaction. The links between natural plant senescence and stress-induced senescence are discussed, as well as the potential role of GS1 and GDH in a metabolic safeguard process.
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PMID:The two senescence-related markers, GS1 (cytosolic glutamine synthetase) and GDH (glutamate dehydrogenase), involved in nitrogen mobilization, are differentially regulated during pathogen attack and by stress hormones and reactive oxygen species in Nicotiana tabacum L. leaves. 1637 36