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PubMed1978

Growth, Phosphate Pools, and Phosphate Mobilization of Salt-stressed Sesame and Pepper.

The growth and phosphate mobilization of control and salt-stressed sesame (Sesamum indicum L.) and pepper (Capsicum annuum L.) plants were examined to ascertain whether or not translocation limits growth of salt-stressed plants. Plants were grown in a complete nutrient solution with and without excess salt. One-half of the control and salt-stressed plants were later transferred to phosphate-free culture solution ("-P" plants). Measurements of growth and phosphate pools in leaves indicated that with or without salinity "-P" plants utilized their phosphate reserves to support growth for a time at rates equaling those of plants supplied with phosphate. The results indicate that mobilization was not limiting for growth of salt-stressed plants.Defoliation experiments were performed at a developmental stage when the import of assimilates by the youngest expanding leaves could be changed by removing certain source or sink leaves. These experiments also indicated that phloem transport was not limiting for leaf growth on salt-stressed plants.

Journal Article↗
PubMed2004

Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate.

The crystal structure of Methanococcus jannaschii 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex with the substrate ribulose 5-phosphate at a dimetal centre has recently been determined at 1.7 A resolution. The enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone 4-phosphate, while its C4 atom is released as formate. The resulting four-carbon body supplies all eight C atoms for the xylene moiety of riboflavin. Three of the four hydroxyl groups of ribulose 5-phosphate were coordinated by the metal ions. Based on crystallographic refinement, the metals were assigned as zinc and calcium, which were present in the crystallization buffer. Neither metal supports the enzymatic reaction. In the present study, the correctness of this assignment is assessed using anomalous diffraction data collected at the high-energy side of the zinc absorption edge (lambda = 1.2823 A). Only the three tentative zinc ions give strong peaks in an anomalous difference Fourier map (>20sigma), whereas the four tentative calcium ions do not show anomalous signals above the noise level. These results confirm the initial assignment. In addition, the resolution was improved to 1.55 A.

Binding Sites↗
PubMed1994

Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis.

The glmU gene product of Escherichia coli was recently identified as the N-acetylglucosamine-1-phosphate uridyltransferase activity which catalyzes the formation of UDP-N-acetylglucosamine, an essential precursor for cell wall peptidoglycan and lipopolysaccharide biosyntheses (D. Mengin-Lecreulx and J. van Heijenoort, J. Bacteriol. 175:6150-6157, 1993). Evidence that the purified GlmU protein is in fact a bifunctional enzyme which also catalyzes acetylation of glucosamine-1-phosphate, the preceding step in the same pathway, is now provided. Kinetic parameters of both reactions were investigated, indicating in particular that the acetyltransferase activity of the enzyme is fivefold higher than its uridyltransferase activity. In contrast to the uridyltransferase activity, which is quite stable and insensitive to thiol reagents, the acetyltransferase activity was rapidly lost when the enzyme was stored in the absence of reducing thiols or acetyl coenzyme A or was treated with thiol-alkylating agents, suggesting the presence of at least one essential cysteine residue in or near the active site. The acetyltransferase activity is greatly inhibited by its reaction product N-acetylglucosamine-1-phosphate and, interestingly, also by UDP-N-acetylmuramic acid, which is one of the first precursors specific for the peptidoglycan pathway. The detection in crude cell extracts of a phosphoglucosamine mutase activity finally confirms that the route from glucosamine-6-phosphate to UDP-N-acetylglucosamine occurs via glucosamine-1-phosphate in bacteria.

Acetyltransferases↗
PubMed1978

Growth of Escherichia coli on glucosamine 6-phosphate: selection of a constitutive hexose phosphate transport system mutant.

Glucosamine 6-phosphate was found to be a substrate but not an inducer for the hexose phosphate transport system of Escherichia coli. Wild-type cells grow very poorly on glucosamine 6-phosphate. A mutant was selected that will grow rapidly on glucosamine 6-phosphate because it contains a constitutive hexose phosphate transport system.

Biological Transport, Active↗
PubMed1990

Kinetic studies of alkyl-dihydroxyacetone-phosphate (alkyl-glycerone-phosphate) synthase in peroxisomes of rat liver.

The properties of peroxisomal enzyme alkylglycerone-phosphate synthase were studied in highly purified peroxisome fractions of rat liver. The requirements for optimal enzyme activity: pH and composition of the reaction mixture, incubation time, and enzyme concentration were investigated, and kinetic studies performed employing both different long-chain fatty alcohols and acyl dihydroxyacetone phosphates as substrates. Activities of the synthase considerably higher as reported before were found in the peroxisome preparation, with alkylglycerone (alkyldihydroxyacetone) phosphate as the sole product of the exchange reaction. The kinetic studies revealed divergent properties of peroxisomal synthase with respect to the substrates involved. Whereas the substrate concentration versus reaction velocity plot for the fatty alcohols reflects Michaelis-Menten kinetic behavior, it displays a maximum followed by inhibition with regard to the acylglycerone phosphate. The enzyme accepts different acylglycerone phosphates without much specificity but it is most active with 9-cis-octadecenol.

Alkyl and Aryl Transferases↗
PubMed1989

Ligand interactions of the cation-independent mannose 6-phosphate receptor. The stoichiometry of mannose 6-phosphate binding.

The interaction of the bovine cation-independent mannose 6-phosphate receptor with a variety of phosphorylated ligands has been studied using equilibrium dialysis and immobilized receptor to measure ligand binding. The dissociation constants for mannose 6-phosphate, pentamannose phosphate, bovine testes beta-galactosidase, and a high mannose oligosaccharide with two phosphomonoesters were 7 X 10(-6) M, 6 X 10(-6) M, 2 X 10(-8) M, and 2 X 10(-9) M, and the mol of ligand bound/mol of receptor monomer were 2.17, 1.85, 0.9, and 1.0, respectively. We conclude that the cation-independent mannose 6-phosphate receptor has two mannose 6-phosphate-binding sites/polypeptide chain.

Acetylglucosamine↗
PubMed1987

Enhanced myocardial protection with high-energy phosphates in St. Thomas' Hospital cardioplegic solution. Synergism of adenosine triphosphate and creatine phosphate.

The potential for improving myocardial protection with the high-energy phosphates adenosine triphosphate and creatine phosphate was evaluated by adding them to the St. Thomas' Hospital cardioplegic solution in the isolated, working rat heart model of cardiopulmonary bypass and ischemic arrest. Dose-response studies with an adenosine triphosphate range of 0.05 to 10.0 mmol/L showed 0.1 mmol/L to be the optimal concentration for recovery of aortic flow and cardiac output after 40 minutes of normothermic (37 degrees C) ischemic arrest (from 24.1% +/- 4.4% and 35.9% +/- 4.1% in the unmodified cardioplegia group to 62.6% +/- 4.7% and 71.0% +/- 3.0%, respectively, p less than 0.001). Adenosine triphosphate at its optimal concentration (0.1 mmol/L) also reduced creatine kinase leakage by 39% (p less than 0.001). Postischemic arrhythmias were also significantly reduced, which obviated the need for electrical defibrillation and reduced the time to return of regular rhythm from 7.9 +/- 2.0 minutes in the control group to 3.5 +/- 0.4 minutes in the adenosine triphosphate group. Under more clinically relevant conditions of hypothermic ischemia (20 degrees C, 270 minutes) with multidose (every 30 minutes) cardioplegia, adenosine triphosphate addition improved postischemic recovery of aortic flow and cardiac output from control values of 26.8% +/- 8.4% and 35.4% +/- 6.3% to 58.0% +/- 4.7% and 64.4% +/- 3.7% (p less than 0.01), respectively, and creatine kinase leakage was significantly reduced. Parallel hypothermic ischemia studies (270 minutes, 20 degrees C) using the previously demonstrated optimal creatinine phosphate concentration (10.0 mmol/L) gave nearly identical improvements in recovery and enzyme leakage. The combination of the optimal concentrations of adenosine triphosphate and creatine phosphate resulted in even greater myocardial protection; aortic flow and cardiac output improved from their control values of 26.8% +/- 8.4% and 35.4% +/- 6.3% to 79.7% +/- 1.1 and 80.7% +/- 1.0% (p less than 0.001), respectively. In conclusion, both extracellular adenosine triphosphate and creatine phosphate alone markedly improve the cardioprotective properties of the St. Thomas' Hospital cardioplegic solution during prolonged hypothermic ischemic arrest, but together they act additively to provide even greater protection.

Adenosine Triphosphate↗
PubMed1976

Inhibition of glycolysis in brain by a phospholipid effect on interconversion of fructose phosphates. A possible regulatory control on utilization of glucose 6-phosphate.

Glucose 6-phosphate accumulation in 10,000 X g supernatant of rat brain was enhanced up to 16-fold by the addition of phosphatidylcholine, other common phospholipids, or linoleate. This glucose 6-phosphate is of endogenous origin via UDP-glucose and glucose 1-phosphate but not glucose. The accumulation is the result of inhibition of glycolysis by an effect of phospholipid on the interconversion of fructose 6-phosphate and fructose 1,6-bisphosphate. Brain is therefore capable of gluconeogenesis from fructose 1,6-bisphosphate. A regulatory function for phospholipid which coordinates glycolysis and other major routes of utilization of glucose 6-phosphate in brain, e.g. inositol synthesis, is proposed.

Animals↗
PubMed1995

Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase.

Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.

Amino Acid Sequence↗
PubMed1975

A mutant of Escherichia coli auxotrophic for organic phosphates: evidence for two defects in inorganic phosphate transport.

An inorganic phosphate transport mutant has been isolated as a sn-glycerol-3-phosphate auxotroph and characterized genetically. Two lesions are responsible for the transport defect. One lesion, pst, is located at minute 74 of the E. coli genetic map while the other lesion, pit, is located at minute 68. All "K10" strains that were examined carry the pit lesion. Evidence is presented that the glycerol phosphate and hexose phosphate transport systems are not important inorganic phophate transport systems. The mapping data indicate that the genetic distance between malA and xyl is greater than that now allowed.

Bacterial Proteins↗
PubMed1988

Relation between intestinal alkaline phosphatase activity and brush border membrane transport of inorganic phosphate, D-glucose, and D-glucose-6-phosphate.

In order to evaluate the role of the alkaline phosphatase in intestinal transport processes, we studied the influence of known modulators of the alkaline phosphatase (polyclonal anti-calf AP antibodies, theophylline and zinc ions) on the absorption rate of glucose, inorganic phosphate and glucose liberated from glucose-6-phosphate into calf duodenal brush border membrane vesicles. Our results allow the following conclusions: First a direct involvement of the AP in the Na+-dependent glucose absorption is unlikely. Indeed, theophylline inhibits strongly the AP activity but rather stimulates the glucose uptake; second the AP is indirectly involved in glucose absorption from glucose-6-phosphate, if its enzymatic hydrolysis is the only source of glucose. In that case the Na+-dependent uptake of glucose was completely suppressed either by phosphatase specific antibodies or by theophylline; third the positive correlation found with calf intestinal BBMV between the inhibition of AP by AP antibodies or by theophylline and the decrease of rate of Na+-dependent Pi uptake rate suggests that the enzyme plays some role in the Pi absorption. It appears from the present study that the AP is probably not a carrier protein itself, but its hydrolytic activity might nevertheless be important for intestinal absorption. After hydrolysis of phosphoric esters the alcohol residues and Pi can be supplied to their specific carriers. Furthermore, the high Pi affinity of the enzyme at physiological pH values, could even favour a transient sequestration of phosphate, which then could be transferred to the Pi carrier.

Acetates↗
PubMed1997

Urease-induced crystallizations of calcium phosphate and magnesium ammonium phosphate in synthetic urine and human urine.

An aggregometer technique was used to study urease-induced crystallizations in synthetic urine and human urine from healthy subjects and patients with chronic spinal cord injuries. The two different phases of crystallization, calcium phosphate and magnesium ammonium phosphate, were easily evaluated with a single assay using this technique. The crystallization of calcium phosphate and magnesium ammonium phosphate varied markedly among the different urine specimens after incubation with urease. The turbidity curves from human urine were divided into four patterns. We assumed that the variations in the patterns of the turbidity curves appeared to be mainly due to differences in the composition of the urine and in the original pH, and that the calcium and magnesium concentrations were very important in the urinary constituents.

Calcium Phosphates↗
PubMed1991

Resolution-enhanced Fourier transform infrared spectroscopy study of the environment of phosphate ion in the early deposits of a solid phase of calcium phosphate in bone and enamel and their evolution with age: 2. Investigations in the nu3PO4 domain.

Resolution-enhanced Fourier Transform Infrared (FTIR) spectra of early mineral deposits in enamel and bone show bands at 1020, 1100, 1110, 1125, and 1145 cm-1 in the nu3PO4 domain which do not belong to well crystallized stoichiometric hydroxyapatite. Bands at 1020 and 1100 cm-1 have been shown to occur in nonstoichiometric apatites containing HPO4(2-) ions and the weak band at 1145 cm-1 has been assigned to HPO4(2-) ions. Though the bands at 1110 and 1125 cm-1 have not been found in any well crystallized apatite, they are present in newly precipitated apatite. These latter bands disappear progressively during maturation in biological as well as synthetic samples, and partial dissolution of synthetic apatites shows that they belong to species that exhibit an inhomogeneous distribution in the mineral, and that are the first to be solubilized. Comparison of the FTIR spectra of biological apatites with those of synthetic, nonapatitic-containing phosphate minerals shows that the presence of these bands does not arise from nonapatitic, well-defined phases; they are due to the local environment of phosphate ions which may possibly be loosely related or perhaps unrelated to the phosphate groups present in the well-crystallized nonapatitic calcium phosphates. Resolution-enhanced FTIR affords a very precise characterization of the mineral phases which may be very useful in characterizing pathological deposits of Ca-P mineral phases.

Animals↗
PubMed2005

Formation of apatitic calcium phosphates in a Na-K-phosphate solution of pH 7.4.

Poorly crystalline, apatitic calcium phosphate powders have been synthesized by slowly adding a Na- and K-containing reference phosphate solution with a pH value of 7.4 to an aqueous calcium nitrate solution at 37 degrees C. Nano-particulated apatitic powders obtained were shown to contain small amounts of Na and K, which render them more similar in chemical composition to that of the bone mineral. Precipitated and dried powders were found to exhibit self-hardening cement properties when kneaded in a mortar with a sodium citrate- and sodium phosphate-containing starter solution. The same phosphate solution used in powder synthesis was found to be able to partially convert natural, white and translucent marble pieces of calcite (CaCO3) into calcium-deficient hydroxyapatite upon aging the samples in that solution for 3 days at 60 degrees C. Sample characterization was performed by using scanning electron microscopy, X-ray diffraction, Fourier-transform infrared spectroscopy, inductively-coupled plasma atomic emission spectroscopy, and simultaneous thermogravimetry and differential thermal analysis.

Apatites↗
PubMed1996

Phosphates precipitating from artificial urine and fine structure of phosphate renal calculi.

Phosphates precipitating from artificial urine in the pH range 6-8 were identified using X-ray diffraction, chemical analysis and scanning electron microscopy. The influence of magnesium and citrate on phases precipitating from urine was established. From urine containing a normal quantity of magnesium (around 70 ppm), brushite accompanied by hydroxyapatite (HAP) precipitated at pH < or = 7.0 and struvite with HAP at pH > 7.0. HAP was formed exclusively from magnesium deficient urine at pH 7.0. Newberyite, octacalcium phosphate and whitlockite were not identified. The chemical and phase composition and inner fine structure of 14 phosphate calculi were studied. Three types of stones were distinguished based on their magnesium content: (i) stones rich in magnesium composed of struvite, hydroxyapatite and abundant organic matter, (ii) stones with low magnesium content constituted by calcium deficient hydroxyapatite, up to 5% of struvite, considerable amount of organic matter and occasionally brushite, and (iii) calculi without magnesium consisting of brushite, hydroxyapatite and little organic matter. Conditions prevaling during stone-formation assessed for each type of stone were confirmed by corresponding urinary biochemical data and corroborate the in vitro studies of phosphates precipitation.

Calcium Phosphates↗
PubMed1984

Organic phosphate probes of the avian renal phosphate secretory mechanism.

Parathyroid hormone (PTH) stimulates net renal inorganic phosphate (Pi) secretion in domestic fowl (Gallus domesticus). Recent evidence indicates that secreted Pi is derived from a highly sequestered, presumably organic, phosphate pool. A modified Sperber technique was used to survey the response of domestic fowl to unilateral renal portal infusions of organic phosphate compounds that had been implicated in previous studies of Pi secretion. None of the organic phosphate compounds produced a significant unilateral Pi secretory effect. It is concluded that these compounds neither directly stimulate Pi secretion in normal or parathyroidectomized birds, nor are they rate-limiting for the Pi secretory mechanism in birds infused with PTH.

Animals↗
PubMed1995

A phosphate-repressible, high-affinity phosphate permease is encoded by the pho-5+ gene of Neurospora crassa.

The pho-5+ gene of Neurospora crassa, which encodes a high-affinity phosphate permease, has been cloned and analyzed. The deduced ORF of 1707 nucleotides is interrupted by a single 63-nt intron and codes for a protein of 569 amino acids (aa). This aa sequence has 48% identity with the high-affinity phosphate transporter of Saccharomyces cerevisiae, PHO84. The pho-5 null mutants have no obvious phenotype. Strains which contain a null mutation in pho-4, which encodes an additional high-affinity phosphate permease [Bowman et al., J. Bacteriol. 153 (1983) 292-296], also have no obvious phenotype. However, strains containing mutations in both pho-5 and pho-4 are unable to grow under phosphate-restrictive conditions.

Amino Acid Sequence↗
PubMed1999

Synthesis of phosphono analogues of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate.

The present paper describes the synthetic routes of six phosphono analogues of dihydroxyacetone phosphate and five phosphono analogues of glyceraldehyde 3-phosphate through alpha-, beta- and gamma-hydroxyphosphonate esters precursors containing a protected carbonyl group. In some situations, depending on the sequence used for the deprotection of the phosphonate and carbonyl groups, the aldol/ketol rearrangement allowed the synthesis of either dihydroxyacetone phosphate or glyceraldehyde 3-phosphate analogues from the same precursors. All these analogues are of interest both as active-site probes and as potential substrates for glycolytic enzymes such as fructose 1,6-diphosphate aldolases (EC 4.1.2.13).

Animals↗