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:3.1.4.1 (phosphodiesterase)
18,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When inorganic phosphate is limiting, Arabidopsis has the facultative ability to metabolize exogenous nucleic acid substrates, which we utilized previously to identify insensitive phosphate starvation response mutants in a conditional genetic screen. In this study, we examined the effect of the phosphate analog, phosphite (Phi), on molecular and morphological responses to phosphate starvation. Phi significantly inhibited plant growth on phosphate-sufficient (2 mM) and nucleic acid-containing (2 mM phosphorus) media at concentrations higher than 2.5 mM. However, with respect to suppressing typical responses to phosphate limitation, Phi effects were very similar to those of phosphate. Phosphate starvation responses, which we examined and found to be almost identically affected by both anions, included changes in: (a) the root-to-shoot ratio; (b) root hair formation; (c) anthocyanin accumulation; (d) the activities of phosphate starvation-inducible nucleolytic enzymes, including ribonuclease, phosphodiesterase, and acid phosphatase; and (e) steady-state mRNA levels of phosphate starvation-inducible genes. It is important that induction of primary auxin response genes by indole-3-acetic acid in the presence of growth-inhibitory Phi concentrations suggests that Phi selectively inhibits phosphate starvation responses. Thus, the use of Phi may allow further dissection of phosphate signaling by genetic selection for constitutive phosphate starvation response mutants on media containing organophosphates as the only source of phosphorus.
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PMID:Attenuation of phosphate starvation responses by phosphite in Arabidopsis. 1170 78

Activities of phytase, a pH 6.0 optimum nonspecific phosphomonoesterase and phosphodiesterase assayed toward bis(p-nitrophenyl)phosphate (phosphodiesterase I) and against p-nitrophenylphosphorylcholine (phosphodiesterase II), were partially purified from mycelial extracts of Aspergillus niger AbZ4 cultivated on a molasses medium by a liquid surface fermentation method. After elimination of phosphate from the medium, 7.3- and 3.5-fold enhancements in specific activities of phytase and phosphodiesterase II were observed. Efficacies of mycelial protein fractions in dephosphorylating a wheat-based broiler feed were determined in vitro according to a procedure that simulated digestion in the intestinal tract of poultry. The addition of 0.052 mg of protein from fractions, each of which was high in either pH 6.0 optimum phosphomonoesterase, phosphodiesterase I, phosphodiesterase II, or phytase per gram of a feed sample resulted in the enhancement of phosphorus release by 10, 11, 27, and 88%, respectively. In the presence of an excess of commercial phytase, the addition of the mycelial fraction high in phytase increased the dephosphorylation rate by 56%. The fraction high in phosphodiesterase II enhanced feed dephosphorylation by 8% in the presence of an excess of commercial phytase and commercial acid phosphatase.
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PMID:In vitro efficacies of phosphorolytic enzymes synthesized in mycelial cells of Aspergillus niger AbZ4 grown by a liquid surface fermentation. 1182 65

Glycerophosphocholine (GroPCho) is a diester that accumulates in different physiological processes leading to phospholipid remodeling. However, very little is known about its metabolism in higher plant cells. (31)P-Nuclear magnetic resonance spectroscopy and biochemical analyses performed on carrot (Daucus carota) cells fed with GroPCho revealed the existence of an extracellular GroPCho phosphodiesterase. This enzymatic activity splits GroPCho into sn-glycerol-3-phosphate and free choline. In vivo, sn-glycerol-3-phosphate is further hydrolyzed into glycerol and inorganic phosphate by acid phosphatase. We visualized the incorporation and the compartmentation of choline and observed that the major choline pool was phosphorylated and accumulated in the cytosol, whereas a minor fraction was incorporated in the vacuole as free choline. Isolation of plasma membranes, culture medium, and cell wall proteins enabled us to localize this phosphodiesterase activity on the cell wall. We also report the existence of an intracellular glycerophosphodiesterase. This second activity is localized in the vacuole and hydrolyzes GroPCho in a similar fashion to the cell wall phosphodiesterase. Both extra- and intracellular phosphodiesterases are widespread among different plant species and are often enhanced during phosphate deprivation. Finally, competition experiments on the extracellular phosphodiesterase suggested a specificity for glycerophosphodiesters (apparent K(m) of 50 microM), which distinguishes it from other phosphodiesterases previously described in the literature.
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PMID:Glycerophosphocholine metabolism in higher plant cells. Evidence of a new glyceryl-phosphodiester phosphodiesterase. 1222 4

Even though fungal phosphatases are widely used to study ambient-regulated gene expression, little is known about these enzymes in the agriculturally important genus Colletotrichum. We have therefore identified several phosphatase activities in endophytic isolates of Colletotrichum musae grown under conditions of nutritional sufficiency or starvation for sources of phosphorus (P), nitrogen (N), carbon (C), and sulphur (S). These enzyme forms could be distinguished by substrate specificity, optimum pH, activation and inhibition by some substances, response to nutritional starvation, and pattern of migration in native gel electrophoresis. At least four individual phosphatase activities were identified under the growth conditions employed. A pH 5.0 acid phosphatase and an Mg(2+)-dependent pH 7.5 phosphodiesterase were expressed under all growth conditions at constant rates. Under conditions of P-starvation, derepression of a major pH 6.0-acid phosphatase was observed in cell-free extracts and the culture medium. A synthesis of alkaline phosphatase activities followed a more distinct pattern. Under conditions of nutritional sufficiency of P- or N-starvation, only a single intracellular enzyme form (optimum pH 10) was observed, which was resolved as a single electrophoretic activity band. However, in media lacking C or S sources additional alkaline phosphatase forms were derepressed with a concomitant increase in the overall enzyme activity level measured at pH 10. To our knowledge, this report represents the most detailed study of phosphatases in Colletotrichum and the first partial characterization of the phosphatase system in an endophytic fungus.
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PMID:Synthesis and secretion of phosphatases by endophytic isolates of Colletotrichum musae grown under conditions of nutritional starvation. 1250 5

Recombinant phospholipase D (PLD) from Streptomyces chromofuscus (scPLD) has been characterized using colorimetric assays, spectroscopic investigations, and site-directed mutagenesis. scPLD, which shows phosphodiesterase activity toward a wide variety of phospholipids and phosphatase activity toward p-nitrophenyl phosphate, exhibits a visible absorption band with lambda(max) at 570 nm. Metal ion analysis performed by inductively coupled plasma mass spectroscopy shows the presence of approximately 1 equivalent of iron, 0.27 equivalent of manganese, and 0.1 equivalent of zinc per mole of protein as isolated. The metal ion content coupled with the visible absorption feature is compatible with the presence of Fe(3+)-tyrosinate coordination. When scPLD was dialyzed against solutions containing Mn(2+), Zn(2+) or EDTA, the Fe(3+) content was reduced to variable extents, and the residual specific activity correlated well with the residual iron content. Sequence homology with metal ion binding motifs in known alkaline phosphatases and purple acid phosphatase from red kidney bean shows that most of the residues involved in metal ion coordination are conserved among all the sequences considered. Mutation of some of these conserved residues (C123A, D151A, Y154F, and H391A) produced enzymes lacking iron with dramatically reduced PLD activity but little change in secondary structure or ability to bind to small unilamellar vesicles of phosphatidylcholine (with Ba(2+)) or phosphatidic acid. We suggest that scPLD is a member of a family of phosphodiesterase/phosphatases with structural and mechanistic similarity to iron-dependent purple acid phosphatases.
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PMID:An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases. 1251 26

We have previously purified and characterized a diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin seeds. This report describes an efficient strategy for overexpression in baculovirus-infected Spodoptera frugiperda Sf9 cells and purification of a functional PPD1 enzyme. We tested six variants of recombinant PPD1, differing in secretion peptides, fusion tags, and promoters. The highest expression level of the active PPD1 was achieved when the native signal peptide and the C-terminal V5-6His tag were attached. This recombinant protein was secreted at very high level (18.4 mg/L) to serum-free medium. Single-step purification procedure using metal affinity chromatography resulted in the homogeneous PPD1. The overexpressed protein showed enzymatic activity comparable to the native enzyme isolated previously from plant material. We showed that PPD1, which belongs to purple acid phosphatase family, formed tetrameric structure, which is non-typical for this group of enzymes.
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PMID:Expression and purification of active plant diphosphonucleotide phosphatase/phosphodiesterase from baculovirus-infected insect cells. 1559 67

We present evidence that protein bodies constitute the principal lytic compartment in storage parenchyma cells of mung bean cotyledons and propose that they play a role in cellular autophagy. We developed a method to isolate protein bodies by incubating tissue slices with cell wall-degrading enzymes and fractionating the cellular organelles on a Ficoll gradient. About 75-80% of the protein bodies present in the protoplasts were recovered intact in a band at the 5/25% Ficoll interface. This band contained a similar proportion of the cellular alpha-mannosidase, N-acetyl-beta-glucosaminidase, ribonuclease, acid phosphatase, phosphodiesterase, and phospholipase D. beta-Amylase was present in the cells but not in the protein bodies. Ultrastructural observations showed that on the 3rd day of seedling growth protein bodies contain small vesicles (0.3-1.0 mum) with a cytoplasmic content (ribosomes, membrane vesicles, mitochondria). Later in seedling growth these vesicles appeared empty. We believe that these are autophagic vesicles resulting from invaginations of the protein body membrane and that their cytoplasmic contents are digested by the acid hydrolases present in the protein bodies.
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PMID:Protein bodies of mung bean cotyledons as autophagic organelles. 1659 58

Protoplasts from 8- to 9-day-old wheat (Triticum aestivum L.) leaves were used to isolate organelles which were examined for their contents of peptide hydrolase enzymes and, in the case of vacuoles, other acid hydrolases. High yields of intact chloroplasts were obtained using both equilibrium density gradient centrifugation and velocity sedimentation centrifugation on sucrose-sorbitol gradients. Aminopeptidase activity was found to be distributed, in approximately equal proportions, between the chloroplasts and cytoplasm. Leucyltyrosine dipeptidase was mainly found in the cytoplasm, although about 27% was associated with the chloroplasts. Vacuoles shown to be free from Cellulysin contamination contained all of the protoplast carboxypeptidase and hemoglobin-degrading activities. The acid hydrolases, phosphodiesterase, acid phosphatase, alpha-mannosidase, and beta-N-acetylglucosamidase were found in the vacuole to varying degrees, but no beta-glucosidase was localized in the vacuole.
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PMID:Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves. 1666 52

Potential impact of different levels and sources of organic composts on activities of phosphatases (acid and alkaline phosphatase, phosphodiesterase, and inorganic pyrophosphatase) was studied after three years of continuous application. Enzyme activities were compared with microbial biomass P and available P. Experimental plots were divided based on the organic source into three groups: those receiving farmyard manure (FYM), vermicompost (VC) and Lantana compost (LC). Microbial biomass P (11.7 g kg(-1) soil), available P (24.0 g kg(-1) soil) and acid phosphatase (1.3 mg g(-1) p-NP g(-1) soil h(-1)) was highest in highest dose of VC. Acid phosphatase activity was high in all plots, including those where microbial biomass P levels were low. Most of the phosphatase activities were significantly correlated with available P in FYM and VC. These relationships were negative for LC treatments. Results showed that application of earthworm casts is helpful in faster transformation of organic P by facilitating better environment to microbes and plant roots.
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PMID:Relative changes in phosphatase activities as influenced by source and application rate of organic composts in field crops. 1750 14

The study was undertaken to determine the impact of high-metal composts on the activities of four soil enzymes. High concentrations of metal salts (Cr, Cu, Ni or a Co-Mo-Pb combination) were added to feedstocks during the thermophilic stage of composting. These four metal-enriched composts and an unamended control compost were then mixed with soil collected from long-term agriculture plots under organic management or conventional management. The compost-soil mixtures were prepared at two rates (1:1 or 1:3 compost:soil, v/v) and incubated at 20 degrees C for three weeks. These 20 combinations plus the five composts and the two soils were added to pots and incubated for three weeks. Following incubation, soil enzyme activities (acid phosphatase, arysulfatase, dehydrogenase, phosphodiesterase) were measured using traditional assay procedures. Compared to the control, none of the high-metal composts inhibited soil enzyme activity. Notably, the Cu compost treatment produced significantly higher activity of all four enzymes in the soil compared to the control. Previous soil management influenced the activity of three enzymes, arysulfatase and dehydrogenase had greater activity in the organic soil while phosphatase activity was greater in the conventional soil. Increasing the proportion of compost in the pot had a positive effect on phosphodiesterase activity only. In conclusion, the high-metal compost treatments either enhanced or caused no adverse effects on soil enzyme activity.
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PMID:The effects of high metal concentrations in soil-compost mixtures on soil enzymes. 2080 67


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