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At least 955 records · Page 53Linked to original sources
PubMed1975

Site of action of inhibitors of carbon dioxide assimilation by whole lettuce chloroplasts.

The sites of action of several compounds, reported to inhibit CO(2) fixation by chloroplast preparations were located by developing assays in lettuce chloroplasts to test their effect on partial reactions of the carbon cycle and on carbonic anhydrase. The results indicated that: d, l-glyceral-dehyde and 5'-AMP inhibit phosphoribulose kinase or isomerase. 3-Phosphoglyceric acid and 6-phosphogluconate inhibit ribulose diphosphate carboxylase. Azide, Mg(2+), and nitrite inhibit the activity of carbonic anhydrase of lettuce chloroplasts and light-dependent CO(2) fixation by intact chloroplasts with similar sensitivities. None of these inhibited CO(2) fixation in ruptured chloroplasts. It is suggested that the inhibition by azide, nitrite, and magnesium ions of CO(2) fixation by intact chloroplasts is due to their inhibition of the activity of carbonic anhydrase.

Journal Article↗
PubMed1992

Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.

A comparison of the primary structures of NAD(+)-dependent D-lactate dehydrogenase with L-lactate dehydrogenase and L-malate dehydrogenase failed to show any sequence similarity. However, D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, glycerate dehydrogenase from cucumber, D-3-phosphoglycerate dehydrogenase and erythronate 4-phosphate dehydrogenase from Escherichia coli showed 38%, 24%, 24% and 22% amino acid identity, respectively. The profile analysis of the aligned sequences confirmed their relatedness. The hydropathy profiles of the aligned dehydrogenases were almost identical between residues 100-300 indicating largely preserved folding patterns of their polypeptide chains. The data suggest that L- and D-specific 2-hydroxy acid dehydrogenase genes evolved from two different ancestors and thus represent two different sets of enzyme families.

Alcohol Oxidoreductases↗
PubMed1980

Growth of Penicillium janthinellum on glycine as sole carbon and nitrogen source.

Penicillium janthinellum is able to grow on glycine as the sole carbon and nitrogen source. The amino acid is transaminated to glyoxylate which is further metabolised to pyruvate by the glycerate pathway. The reaction product of partially purified glycerate kinase from this fungus is 2-phosphoglycerate. Phosphoglycerate mutase initiates gluconeogenesis from glycine. Partially purified phosphoglycerate mutase is inhibited by fructose 6-phosphate. The possible significance of this regulation is discussed.

Carbon↗
PubMed1979

Active site phosphohistidine peptides from red cell bisphosphoglycerate synthase and yeast phosphoglycerate mutase.

Bisphosphoglycerate synthase (glycerate-1,3-P2 yields glycerate-2,3-P2) and phosphoglycerate mutase (glycerate-3-P formed from glycerate-2-P) are both phosphorylated by substrates at a histidine residue forming covalent intermediates which have been shown to function in the phosphoryl transfer reactions catalyzed by these enzymes (Rose, Z. B., and Dube, S. (1976) J. Biol. Chem. 251, 4817--4822). We have phosphorylated bisphosphoglycerate synthase from horse red blood cells with [U-32P]glycerate-2,3-P2, digested with trypsin, and purified the phosphopeptide. The amino acid sequence of the phosphohistidine peptide has been determined to be: His-Gly-Gln-Gly-Ala-Trp-Asn-Lys. In like manner, a phosphohistidyl peptide has now been purified from yeast phosphoglycerate mutase, for which the amino acid sequence is known (Winn, S. I., Watson, H. C., Fothergill, L. A., and Harkins, R. N. (1977) Biochem. Soc. Trans. 5, 657-659). The amino acid composition of the phosphopeptide indicates that histidine-8 was phosphorylated. The sequence of this peptide is closely homologous with the active site peptide from bisphosphoglycerate synthase. In yeast phosphoglycerate mutase, the denatured phosphoenzyme hydrolyzes with a single rate constant of 2.02 X 10(-4) s-1 at pH 3, 45 degrees C. The relevance of these observations to the enzymatic mechanism is discussed.

Amino Acid Sequence↗
PubMed1984

ATP-dependent phosphorylation of alpha-substituted carboxylic acids catalyzed by pyruvate kinase.

Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate (F. J. Kayne (1974) Biochem. Biophys. Res. Commun. 59, 8-13). An investigation of anologous reactions with other alpha-substituted carboxylic acids reveals several new substrates for such a phosphorylation reaction. Thus the alpha-hydroxy carboxylic acids L-lactate, D-lactate, DL-alpha-hydroxybutyrate, DL-alpha-hydroxyvalerate, L-glycerate, D-glycerate, DL-nitrolactate, and DL-beta-chlorolactate are phosphorylated on the alpha-hydroxy group to give the corresponding phosphoesters. Thioglycolate is also a slow substrate for phosphorylation of the thiol group to give the phosphothioglycolate, and DL-thiolactate is phosphorylated in a very slow reaction to give phosphothiolactate. beta-Hydroxypyruvate is a substrate; but, unlike the reaction with pyruvate, with beta-hydroxypyruvate the equilibrium for the reaction lies in favor of ADP and the phosphorylated product which appears from 31P NMR data to be tartronate-semialdehyde-2-phosphate. 31P NMR spectroscopy has been used to verify the identity of the products for all of the reactions. Steady-state kinetic constants have been obtained for some of the more rapid reactions. The reactions with glycolate, L-glycerate, and beta-hydroxypyruvate have kcat values that are close to that for phosphorylation of pyruvate in the reverse of the physiological reaction.

Adenosine Triphosphate↗
PubMed1992

Transfer of deuterium from [1,1-2H2]ethanol to steroids and organic acids in the rat testis.

Rats were given [1,1-2H2]ethanol in a single dose, and the 2H content was determined in testicular steroids and in organic acids of low molecular mass in the testis, liver and blood. The acids were quantified by capillary gas chromatography/mass spectrometry of t-butyldimethylsilyl derivatives with [2H4]lactate as internal standard. In addition to lactate, pyruvate, 3-hydroxybutyrate and acids of the tricarboxylic acid cycle, the testis was shown to contain 2-hydroxybutyrate, 2-hydroxy-2-methylbutyrate, 2-hydroxyisohexanoate and glycerate. No 2H was found in pregnenolone, 5-androstene-3 beta,17 beta-diol or testosterone, whereas the abundance of monodeuterated molecules of 5 alpha-androstane-3 alpha,17 beta-diol and its 3 beta-isomer were 7.6% and 11.2% respectively. The abundance of monodeuterated lactate was 7.0% in the testis and 5.3% in the blood. The other acids were less labelled but 3-hydroxybutyrate had a higher 2H content in the testis (3.1%) than in the liver. These results support the contention that ethanol is oxidized in an alcohol dehydrogenase-catalysed reaction in testis in vivo and that the acute inhibition of the testosterone production is due at least partly to a redox effect. The labelling and increased concentration of 3-hydroxybutyrate in the testis indicate that a change in the mitochondrial redox state might be involved.

Animals↗
PubMed1966

Purification and properties of two glyoxylate reductases from a species of Pseudomonas.

1. Two enzymes that catalyse the reduction of glyoxylate to glycollate have been separated and purified from a species of Pseudomonas. Their molecular weights were estimated as 180000. 2. Reduced nicotinamide nucleotides act as the hydrogen donators for the enzymes. The NADH-linked enzyme is entirely specific for its coenzyme but the NADPH-linked reductase shows some affinity towards NADH. 3. Both enzymes convert hydroxypyruvate into glycerate. 4. The glyoxylate reductases show maximal activity at pH6.0-6.8, are inhibited by keto acids and are strongly dependent on free thiol groups for activity. 5. The Michaelis constants for glyoxylate and hydroxypyruvate were found to be of a high order. 6. The reversibility of the reaction has been demonstrated for both glyoxylate reductases and the equilibrium constants were determined. 7. The reduction of glyoxylate and hydroxypyruvate is not stimulated by anions.

Journal Article↗
PubMed1978

Neuronal, non-neuronal and hybrid forms of enolase in brain: structural, immunological and functional comparisons.

Three forms of the glycolytic enzyme, enolase [2-phospho-D-glycerate hydrolase (E.C. No. 4.2.1.11)] have been prepared from rat whole brain extract. The most acidic enolase form is neuron specific enolase (NSE) which had previously been designated neuron specific protein (NSP). The least acidic form designated non-neuronal enolase (NNE) has been purified and compared structurally, immunologically and functionally to NSE. NNE is a dimer of 86,500 M.W. consistint of two very similar subunits. The data establish that NNE is larger than NSE which has been shown to be composed of two apparently identical 39,000 molecular weight subunits (78,000). NNE is less acidic than NSE having a pI of 5.9 compared to the value of 4.7 for NSE. Structural and immunological analysis establishes that the NNE subunit is distinct from the NSE subunit, and are therfore products of two separate genes. The structural designation of NSE is (gammagamma) and that of NNE (alpha' alpha'). NSE is strictly localized in neurons indicating that the gene coding for the gamma subunit is only expressed in neuronal cells. The intermediate brain enolase form has been partially purified; structural and immunological evidence indicate that it is a hybrid molecule consisting of one NNE subunit and one NSE subunit (alpha'gamma).

Amino Acid Sequence↗
PubMed2005

Identification of Darmstoff analogs as selective agonists and antagonists of lysophosphatidic acid receptors.

Darmstoff describes a family of gut smooth muscle-stimulating acetal phosphatidic acids initially isolated and characterized from the bath fluid of stimulated gut over 50 years ago. Despite similar structural and biological profiles, Darmstoff analogs have not previously been examined as potential LPA mimetics. Here, we report a facile method for the synthesis of potassium salts of Darmstoff analogs. To understand the effect of stereochemistry on lysophosphatidic acid mimetic activity, synthesis of optically pure stereoisomers of selected Darmstoff analogs was achieved starting with chiral methyl glycerates. Each Darmstoff analog was evaluated for subtype-specific LPA receptor agonist/antagonist activity, PPARgamma activation, and autotaxin inhibition. From this study we identified compound 12 as a pan-antagonist and several pan-agonists for the LPA(1-3) receptors. Introduction of an aromatic ring in the lipid chain such as analog 22 produced a subtype-specific LPA(3) agonist with an EC(50) of 692 nM. Interestingly, regardless of their LPA(1/2/3) ligand properties all of the Darmstoff analogs tested activated PPARgamma. However, these compounds are weak inhibitors of autotaxin. The results indicate that Darmstoff analogs constitute a novel class of lysophosphatidic acid mimetics.

Animals↗
PubMed1970

The pathway of glycollate utilization in Chlorella pyrenoidosa.

1. Exogenous glycollate was rapidly metabolized in both the light and the dark by photoautotrophically grown Chlorella pyrenoidosa. 2. The incorporation of (14)C from [1-(14)C]glycollate by these cells was inhibited by the tricarboxylic acid-cycle inhibitors monofluoroacetate, diethylmalonate and arsenite, and also by alpha-hydroxypyrid-2-ylmethanesulphonate and isonicotinylhydrazine. 3. Short-term kinetic experiments showed over 80% of the total (14)C present in the soluble fraction from the cells to be in glycine and serine after 10s. This percentage decreased with time whereas the percentage radioactivity in glycerate increased for up to 30s then remained steady. The percentage of the total radioactivity present in citrate increased over the experimental period. Malate was the only other tricarboxylic acid-cycle intermediate to become labelled. 4. The kinetic and inhibitor experiments supported the following pathway of glycollate incorporation: glycollate --> glyoxylate --> glycine --> serine --> hydroxypyruvate --> glycerate --> 3-phosphoglycerate --> 2-phosphoglycerate --> phosphoenolpyruvate --> pyruvate --> acetyl-CoA. 5. The specific activities of the enzymes catalysing this metabolic sequence in cell-free extracts were great enough to account for the observed rate of glycollate metabolism of 0.25mumol/h per mg dry wt. of cells in the light.

Carbon Isotopes↗
PubMed1978

Microbial metabolism of aliphatic glycols. Bacterial metabolism of ethylene glycol.

A species of Flavobacterium isolated from pond water by its ability to grow aerobically on ethylene glycol as the role source of carbon initially oxidised the diol to glyoxylate via glycollate. The glyoxylate was metabolised by the glycerate pathway to acetyl-CoA. The acetyl-CoA was further metabolised by the tricarboxylic acid cycle plus malate synthase acting anaplerotically.

Culture Media↗
PubMed1976

Isolation and partial characterization of monophosphoglycerate mutase from human erythrocytes.

Monophosphoglycerate mutase has been purified to homogeneity from outdated human erythrocytes as indicated by exclusion chromatography, polyacrylamide gel electrophoresis, and equilibrium centrifugation. Occasionally, the recommended purification procedure yields a small amount (3% or less) of a single extraneous protein which can be deleted from the enzyme preparation by employing an additional purification step. The native enzyme has a molecular weight of 54,000 to 56,000 as determined by equilibrium centrifugation and exclusion chromatography. Disc gel electrophoresis in the presence of sodium dodecyl sulfate yields a single protein band with a molecular weight of 28,600, indicating that the native macromolecule is a dimer composed of subunits of similar mass. Homogeneous monophosphoglycerate mutase is free of diphosphoglycerate mutase, enolase, and nonspecific phosphatase activities; however, the enzyme manifests intrinsic 2,3-diphospho-D-glycerate phosphatase activity as shown by thermal denaturation studies. The diphosphatase activity is stimulated by PPi and glycolate-2-P, but is inhibited by Cl-, HSO3-, and Pi. The pH optimum for both the diphosphatase and the mutase is 6.8. The Km for 2,3-diphospho-D-glycerate in the phosphatase reaction is 82 muM at 37 degrees and pH 7.2. The amino acid composition of homogeneous monophosphoglycerate mutase is given.

Amino Acids↗
PubMed1995

Mutagenesis of an amino acid residue in the activator-binding site of cyanobacterial ADP-glucose pyrophosphorylase causes alteration in activator specificity.

The specificity for activator of ADP-glucose pyrophosphorylase is closely related to the corresponding major carbon-assimilation pathway. The enzyme from Escherichia coli is mainly activated by fructose-1,6-P2, while the cyanobacterial, algal, and higher-plant enzymes are activated by 3-P-glycerate. Previous results have shown that Lys39 of the E. coli enzyme is involved in the binding of fructose-1,6-P2 while for the Anabaena enzyme, lysine residues 382 and 419 have been shown to be involved in the binding of 3-phosphoglycerate. This report shows that if Lys419 of the Anabaena enzyme is changed to glutamine, activation of the cyanobacterial enzyme by fructose-1,6-P2 becomes more effective than that of 3-P-glycerate at lower concentrations. Kinetic studies show that fructose-1,6-P2 competitively inhibits 3-P-glycerate activation of the Anabaena wild-type enzyme, suggesting that these two compounds bind to the same site. Thus a change of one amino acid at the activator binding domain can affect the specificity of activation of the Anabaena ADP-glucose pyrophosphorylase.

Allosteric Regulation↗
PubMed1999

Facile syntheses for (5Z,9Z)-5,9-hexadecadienoic acid, (5Z,9Z)-5,9-nonadecadienoic acid, and (5Z,9Z)-5,9-eicosadienoic acid through a common synthetic route.

The delta 5,9 fatty acids (5Z,9Z)-5,9-hexadecadienoic acid, (5Z,9Z)-5,9-nonadecadienoic acid, and (5Z,9Z)-5,9-eicosadienoic acid were synthesized for the first time in four steps (9-12% overall yield) starting from commercially available 2-(2-bromoethyl)-1,3-dioxolane. The synthetic approach provided enough material to corroborate the structure and stereochemistry of (5Z,9Z)-5,9-nonadecadienoic acid which was recently identified in the flowers of Malvaviscus arboreus (Malvaceae). The novel phospholipids 1-hexadecanoyl-2-[(5Z,9Z)-5,9-eicosadienoyl]-sn-glycer o-3-phosphocholine and 1-octadecanoyl-2-[(5Z,9Z)-5,9-eicosadienoyl]-sn- glycero-3-phosphocholine were also synthesized from commercially available L-alpha-phosphatidylcholine (egg yolk) and characterized by positive ion electrospray mass spectrometry. These are the first examples of unsymmetrical phospholipids with saturated fatty acids at the sn-1 position and delta 5,9 fatty acids at the sn-2 position.

Animals↗
PubMed1979

[Respiration at high altitudes, phosphate-protein interaction: the sequence of hemoglobins from guinea pig and dromedary (author's transl)].

The sequence of the main hemoglobin component of the guinea pig (Cavia aerea f. porcellus, Caviidae) and that of the hemoglobin of the dromedary (Camelus dromedarius, Camelidae) is given. The sequence is obtained automatically by the sequenator using the quadrol and the propyne programme. The sequence of the alpha-and beta-chains of the guinea pig is compared with that of the human hemoglobin; the sequence of the dromedary in comparison to the Ilama shows in the alpha-chains five amino acid exchanges, in the beta-chains there are only two exchanges in beta 2 and beta 76. Beta 2 in dromedary is the P2-glycerate contact histidine. This sustains the interpretation of the high altitude respiration of the Ilama as mutation beta2His leads to Asn.

Altitude↗
PubMed1995

Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing.

Enolase (2-phospho-D-glycerate hydrolase; EC 4.2.1.11) from the hyperthermophilic bacterium Thermotoga maritima was purified to homogeneity. The N-terminal 25 amino acids of the enzyme reveal a high degree of similarity to enolases from other sources. As shown by sedimentation analysis and gel-permeation chromatography, the enzyme is a 345-kDa homoctamer with a subunit molecular mass of 48 +/- 5 kDa. Electron microscopy and image processing yield ring-shaped particles with a diameter of 17 nm and fourfold symmetry. Averaging of the aligned particles proves the enzyme to be a tetramer of dimers. The enzyme requires divalent cations in the activity assay, Mg2+ being most effective. The optimum temperature for catalysis is 90 degrees C, the temperature dependence yields a nonlinear Arrhenius profile with limiting activation energies of 75 kJ mol-1 and 43 kJ mol-1 at temperatures below and above 45 degrees C. The pH optimum of the enzyme lies between 7 and 8. The apparent Km values for 2-phospho-D-glycerate and Mg2+ at 75 degrees C are 0.07 mM and 0.03 mM; with increasing temperature, they are decreased by factors 2 and 30, respectively. Fluoride and phosphate cause competitive inhibition with a Ki of 0.14 mM. The enzyme shows high intrinsic thermal stability, with a thermal transition at 90 and 94 degrees C in the absence and in the presence of Mg2+.

Amino Acid Sequence↗
PubMed1993

Assay of Proton-Coupled Glycolate and D-Glycerate Transport into Chloroplast Inner Envelope Membrane Vesicles by Stopped-Flow Fluorescence.

The transport of glycolate and D-glycerate across the inner envelope membrane of intact chloroplasts is rapid and mediated by a translocator with proton/substrate symport activity. The true initial rate of glycolate or D-glycerate transport could not be measured by conventional methods. To resolve the initial rates of glycolate and D-glycerate transport, a stopped-flow fluorescence assay was developed that allows the indirect observation of transport from about 4 ms after mixing. Inner envelope vesicles from pea (Pisum sativum) or spinach (Spinacia oleracea) chloroplasts were loaded with the fluorescent pH indicator pyranine (8-hydroxypyrene-1,3,6-trisulfonic acid) by a freeze-thaw sonication protocol. A rapid quenching of pyranine fluorescence was detected after mixing the vesicles with either glycolate or D-glycerate. This quenching was the result of acidification of the interior of the vesicles. D-Glycerate- or glycolate-induced acidification displayed saturation kinetics and was inhibited by pretreatment of the vesicles with N-ethylmaleimide. D-Glycerate was more effective than L-glycerate in causing the pH decrease. Also, L-mandelate inhibited D-glycerate-induced acidification much more strongly than D-mandelate. The glycolate/D-glycerate-induced pH decrease is consistent with glycolate/D-glycerate translocator activity. The assay was placed on a quantitative basis by converting fluorescence changes to pH and measuring the internal buffering capacity of the vesicles. The rates of transport across the inner envelope membrane were estimated to be as fast, if not faster, than those of transport in intact chloroplasts.

Journal Article↗
PubMed1991

The role of phosphoenolpyruvate carboxykinase in a marine macroalga with C4-like photosynthetic characteristics.

Udotea flabellum is a marine, macroscopic green alga with C4-like photosynthetic characteristics, including little O2 inhibition of photosynthesis, a low CO2 compensation point, and minimal photorespiration; but it lacks anatomical features analogous to the Kranz compartmentation of C4 plants, and phosphoenolpyruvate carboxylase [PEPC; orthophosphate:oxaloacetate carboxy-lyase (phosphorylating), EC 4.1.1.31] activity is negligible. Phosphoenolpyruvate carboxykinase (PEPCK) activity (carboxylating) in Udotea extracts was equivalent to that of ribulose-bisphosphate carboxylase [Rubisco; 3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39]. When PEPCK activity was inhibited in vivo with 3-mercaptopicolinic acid (MPA), thallus photosynthesis decreased by 70% and became sensitive to O2. Codium decorticatum, a related species that lacks C4-like photosynthetic features and PEPCK activity, showed no increase in O2 inhibition upon exposure to MPA. Rubisco and PEPC activities in Udotea were not inhibited by MPA. Labeling of the early photosynthetic products malate and aspartate was reduced 66% by MPA, while intermediates of the photorespiratory carbon oxidation cycle showed a 3-fold increase. Udotea evolved O2 in the light in the absence of inorganic carbon, suggesting it had an endogenous carbon source for photosynthesis. Exogenous malate stimulated this process, while MPA inhibited it. PEPCK was not involved in Crassulacean acid metabolism or dark CO2 fixation. These MPA studies establish a direct link between PEPCK activity and the low O2 inhibition of photosynthesis and low photorespiration in Udotea. The data are consistent with carboxylation by a cytosolic PEPCK providing a C4 acid, such as malate, to the chloroplast for decarboxylation to elevate the CO2 concentration at the Rubisco fixation site. Udotea is to date the most primitive plant with a C4-like form of photosynthesis.

Journal Article↗