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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)

A maize root fraction which inactivates nitrate reductase has been shown to have protease activity which can be measured by the hydrolysis of azocasein. This inactivating enzyme was also found to inactivate yeast tryptophan synthase. Yeast proteases A and B, which inactivate this latter enzyme, also gave a specific inactivation of the maize nitrate reductase. The maize root inactivating enzyme, like yeast protease B, degraded casein, and was inhibited by phenylmethylsulphonyl fluoride. A partially-purified yeast inhibitor prevented catalysis by the yeast proteases and maize root inactivating enzyme, but purified yeast inhibitors were without effect on the latter protein. The level of nitrate reductase-inactivating activity, and associated azocasein-degrading activity, increased with age of the maize root. Evidence was obtained for a heat stable inhibitor which maintained them in an inactive state, especially in the young root tip cells.
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PMID:Comparison of a nitrate reductase-inactivating enzyme from the maize root with a protease form yeast which inactivates tryptophan synthase. 35 1

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

In L. minor grown in sterile culture, the primary enzymes of nitrate assimilation, nitrate reductase (NR), nitrite reductase (NiR) and glutamate dehydrogenase (GDH) change in response to nitrogen source. NR and NiR levels are low when grown on amino acids (hydrolyzed casein) or ammonia; both enzymes are rapidly induced on addition of nitrate, while addition of nitrite induces NiR only. Ammonia represses the nitrate induced synthesis of both NR and NiR.NADH dependent GDH activity is low when grown on amino acids and high when grown on nitrate or ammonia, but the activities of NADPH dependent GDH and Alanine dehydro-genase (AIDH) are much less affected by nitrogen source. NADH-GDH and AIDH are induced by ammonia, and it is suggested that these enzymes are involved in primary nitrogen assimilation.
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PMID:Nitrogen metabolis of Lemna minor. II. Enzymes of nitrate assimilation and some aspects of their regulation. 579 47

The nitrate reductase activities (NRA) of 31 ditelosomic stocks were compared with that of the control plant [Chinese Spring (CS) euploid], using in vivo and in vitro assay procedures that had been optimized with respect to the euploid. Fourteen stock exhibited significant differences in in vivo NRA from that of the euploid; the effect of removal of a chromosome arm was always to increase NRA. Eight of these stocks showed similar effects in vitro, although in three, a casein-sensitive factor had to be eliminated before the difference was expressed. Homoeologous group effects were evident among ditelosomics of groups 2, 4, and 7, while for three chromosomes (2D, 7A, and 7B), removal of either are resulted in a similar increase in NRA in vivo and probable in vitro.
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PMID:Nitrate reductase activity (in vivo and in vitro) of ditelosomic stocks of wheat (Triticum aestivum L.). 719 7

Nitrate reductase from the yeast Candida nitratophila was found to contain one molecule of cytochrome b557 and one atom of molybdenum per subunit. FAD/haem-dependent diaphorase activity (haem domain) was associated with a 40 kDa tryptic fragment of the subunit. The 50 amino-terminal residues of this fragment were determined, and the sequence did not show significant similarity to deduced sequences of other nitrate reductases previously published. Increasing ionic strength in vitro had a stimulatory effect on enzymic activity via stimulation of the molybdenum-dependent terminal nitrate-reducing activity. Stimulation of activity by exogenous protein (bovine serum albumin or casein) also appeared to be an ionic effect. Stimulation of catalytic activity by phosphate was a separate effect.
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PMID:Further characterization of the assimilatory nitrate reductase from the yeast Candida nitratophila. 847 56

A cheese dairy and its whey manufacturing line were examined for Bacillus cereus. Colonies typical of B. cereus were detected in 120 (17%) samples out of 720 analysed. Only 3% of the sampled raw milk contained B. cereus ( > or = 10 cfu ml(-1)) whereas in evaporated whey concentrate B. cereus was present in 76% of the samples. Nitrate reductase negative and weakly casein hydrolysis isolates were rare in raw milk and the early parts of the process but these defective biotypes became increasingly frequent towards the end of the whey process. The composition of whole cell fatty acids of B. cereus isolates originating from the whey part of the process was different from that of the type strain and of the isolates originating from the raw materials of cheese making. The B. cereus strains in concentrated whey were 100% similar to the type strain in 16S rDNA sequence (500 bp) although they were not or only poorly recognized as B. cereus by a commercial whole cell fatty acid library. All of B. cereus isolates in raw milk were sensitive to one or more of the B. cereus group phages (n = 17) whereas 43% of the isolates from the whey process were sensitive to none. None of the 23 strains originating from the whey processing lines grew at < or = 8 degrees C. although strains with minimum growth temperatures of 5.3 degrees C and 7.0 degrees C were present in the raw materials. Our results indicate that the B. cereus population of the warm ( > 30 degrees C) parts of the cheese dairy process was separate from that of cold (2 degrees C to 4 degrees C) part of the process.
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PMID:Bacillus cereus in a whey process. 984 82

The activity and allosteric properties of plant phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) are controlled posttranslationally by specific reversible phosphorylation of a strictly conserved serine residue near the N-terminus. This up/down-regulation of PEPC is catalyzed by a dedicated and highly regulated serine/threonine (Ser/Thr) kinase (PEPC-kinase) and an opposing type-2A Ser/Thr phosphatase (PP2A). In marked contrast to PEPC-kinase, the PP2A holoenzyme from photosynthetic tissue has been virtually unstudied to date. In the present investigation, we have partially purified and characterized the native form of this PP2A from illuminated leaves of maize (Zea mays L.), a C4 plant, using maize [32P]PEPC as substrate. Various conventional chromatographic matrices, together with thiophosphorylated C4 PEPC-peptide and microcystin-LR affinity-supports, were exploited for the enrichment of this PP2A from soluble leaf extracts. Biochemical and immunological results indicate that the C4-leaf holoenzyme is analogous to other eukaryotic PP2As in being a approximately 170-kDa heteromer comprised of a core PP2Ac-A heterodimer (approximately 38- and approximately 65-kDa subunits, respectively) complexed with a putative, approximately 74-kDa B-type regulatory/targeting subunit. This heterotrimer lacks any strict substrate specificity in that it dephosphorylates C4 PEPC, mammalian phosphorylase a, and casein in vitro. This activity is independent of free Me2+, insensitive to levamisole and the Inhibitor-2 protein that targets PP1, activated by several polycations such as protamine and poly-L-lysine, and highly sensitive to inhibition by microcystin-LR and okadaic acid (IC50 approximately 30 pM), all of which are diagnostic features of yeast and mammalian PP2As. In addition, this C4-leaf PP2A holoenzyme (i) is inhibited in vitro by physiological concentrations of certain C4 PEPC-related metabolites (L-malate, PEP, glucose 6-phosphate, but not the activator glycine) when either 32P-labeled maize PEPC or rabbit muscle phosphorylase a is used as substrate, suggesting a direct effect on this Ser/Thr phosphatase; and (ii) displays, at best, only modest light/dark effects in vivo on its apparent molecular mass, component core subunits and activity against C4 PEPC, in marked contrast to the opposing activity of PEPC-kinase in C4 and Crassulacean acid metabolism leaves. This report represents one of the few studies of a heteromeric PP2A holoenzyme from photosynthetic tissue that dephosphorylates a known target enzyme in plants, such as PEPC, sucrose-phosphate synthase or nitrate reductase.
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PMID:Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosophoenolpyruvate carboxylase. 1150 60

Nitrate reductase activity in excised embryos of Agrostemma githago increases in response to both NO(3) (-) and cytokinins. We asked the question whether cytokinins affected nitrate reductase activity directly or through NO(3) (-), either by amplifying the effect of low endogenous NO(3) (-) levels, or by making NO(3) (-) available for induction from a metabolically inactive compartment. Nitrate reductase activity was enhanced on the average by 50% after 1 hour of benzyladenine treatment. In some experiments, the cytokinin response was detectable as early as 30 minutes after addition of benzyladenine. Nitrate reductase activity increased linearly for 4 hours and began to decay 13 hours after start of the hormone treatment. When embryos were incubated in solutions containing mixtures of NO(3) (-) and benzyladenine, additive responses were obtained. The effects of NO(3) (-) and benzyladenine were counteracted by abscisic acid. The increase in nitrate reductase activity was inhibited at lower abscisic acid concentrations in embryos which were induced with NO(3) (-), as compared to embryos treated with benzyladenine. Casein hydrolysate inhibited the development of nitrate reductase activity. The response to NO(3) (-) was more susceptible to inhibition by casein hydrolysate than the response to the hormone. When NO(3) (-) and benzyladenine were withdrawn from the medium after maximal enhancement of nitrate reductase activity, the level of the enzyme decreased rapidly. Nitrate reductase activity increasd again as a result of a second treatment with benzyladenine but not with NO(3) (-). At the time of the second exposure to benzyladenine, no NO(3) (-) was detectable in extracts of Agrostemma embryos. This is taken as evidence that cytokinins enhance nitrate reductase activity directly and not through induction by NO(3) (-).
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PMID:Enhancement of Nitrate Reductase Activity by Benzyladenine in Agrostemma githago. 1665 64

The in vitro instability of nitrate reductase (EC 1.6.6.1) activity from leaves of several species of higher plants was investigated. Decay of activity was exponential with time, suggesting that an enzyme-catalyzed reaction was involved. The rate of decay of nitrate reductase activity increased as leaf age increased in all species studied. Activity was relatively stable in certain genotypes of Zea mays L., but extremely unstable in others. In all genotypes of Avena sativa L. and Nicotiana tabacum L. studied, nitrate reductase was unstable. Addition of 3% (w/v) bovine serum albumin or casein to extraction media prevented or retarded the decay of nitrate reductase activity for several hours. In addition, the presence of bovine serum albumin or casein in the enzyme homogenate markedly increased nitrate reductase activity (up to 15-fold), especially in older leaf tissue.
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PMID:Use of protein in extraction and stabilization of nitrate reductase. 1665 69

The standard procedure for the in ritro extraction of nitrate reductase from the tip region (0-2 cm) of the primary root of the maize (Zea mays L.) seedling indicated an activity of the enzyme approximately 5-fold higher than that obtained with an in vivo assay. In more mature regions of the primary root the ratio of in vitro to in vivo activity was much lower and in older seedlings was less than unity. The mature root extracts had a more labile nitrate reductase and a higher level of an inactivating enzyme. The use of phenylmethylsulphonyl fluoride in the extraction medium gave only a partial protection of the nitrate reductase from the old root samples. Casein (3%) resulted in a greatly increased yield of nitrate reductase (36-fold with one sample) and a more constant in vitro-in vivo activity ratio for all root samples. With casein in the extraction medium, much higher levels of nitrate reductase were recovered from the mature root zone, and the root content of this enzyme was now shown to be quite a significant proportion of the total in the maize seedling. Casein was shown to inhibit the action of the inactivating enzyme on nitrate reductase. Evidence is also presented for a nitrate reductase inactivating enzyme in the maize scutella and leaf tissues and in the roots and shoots of pea seedlings.
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PMID:A Re-evaluation of the Nitrate Reductase Content of the Maize Root. 1665 65


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