Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Glyceric Acids”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 397 records · Page 22Linked to original sources
PubMed1964

QUANTITATIVE STUDIES ON GLYCOLYTIC ENZYMES IN LACTOBACILLUS PLANTARUM. II. INTRACELLULAR CONCENTRATIONS OF GLYCOLYTIC INTERMEDIATES IN GLUCOSE-METABOLIZING WASHED CELLS.

Mizushima, Shôji (University of Tokyo, Tokyo, Japan), and Kakuo Kitahara. Quantitative studies on glycolytic enzymes in Lactobacillus plantarum. II. Intracellular concentrations of glycolytic intermediates in glucose-metabolizing washed cells. J. Bacteriol. 87:1429-1435. 1964.-The intracellular concentrations of glycolytic intermediates in glucose-metabolizing cells could be estimated by using C(14)-glucose of high specific activity. Separation of each intermediate was accomplished by column chromatography with Dowex 1-X8 (formate) ion-exchange resin. If the intermediates were inseparable, one was converted into another substance separable by chromatography. Almost all the glycolytic intermediates were found to be radioactive, and all of the radioactive substances appearing on the chromatograms were limited to glycolytic intermediates or their related substances. The results clearly show the role of the glycolytic system for lactic acid fermentation in the organism. Among the intermediates, fructose-1,6-diphosphate and 3-phosphoglycerate were found to be present in relatively high concentrations. The reason for the high concentrations of these compounds is discussed.

Carbohydrate Metabolism↗
PubMed2003

Structure-based design of novel inhibitors of 3-deoxy-D-manno-octulosonate 8-phosphate synthase.

3-Deoxy-D-manno-octulosonate 8-phosphate (KDO8P) is the phosphorylated precursor of KDO, an essential sugar of the lipopolysaccharide of Gram negative bacteria. KDO8P is produced by a specific synthase (KDO8PS) by condensing arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP), with release of inorganic phosphate. As KDO8PS is present in bacteria and plants, but not in mammalian cells, and mutations that inactivate KDO8PS also block cell replication, KDO8PS is a promising target for the design of new antimicrobials that act by blocking lipopolysaccharide biosynthesis. Previous studies have shown that a compound mimicking an intermediate of the condensation reaction is a good ligand and a powerful inhibitor. Here we report on the crystallographic investigation of the binding to KDO8PS of new derivatives of this original inhibitor. The structures of the enzyme in complex with these compounds, and also with the PEP analogs, 2-phosphoglyceric acid (2-PGA) and Z-methyl-PEP, point to future strategies for the design of novel inhibitors of KDO8PS.

Aldehyde-Lyases↗
PubMed1987

A highly sensitive method for detection of 32P incorporation into acid-soluble compounds and its application to evaluate ATP-forming ability of Bacillus megaterium QM B1551 spores at the very early stage of germination.

A method for specific removal of [32P]orthophosphate (Pi) as phosphomolybdate-triethylamine complex was slightly modified by repeating the Pi precipitation procedures in the presence of unlabeled Pi, which resulted in a complete removal of 32Pi (greater than 99.98%). Using this modified method, we determined 32P incorporation into acid-soluble compounds in order to evaluate the ATP-forming ability of Bacillus megaterium spores at the very early stage of germination. Addition of fructose as a substrate started the 32P incorporation later than a few min after triggering germination. This delay of a few min was well coincident with the onset of 3-phosphoglycerate (3PGA) breakdown, indicating that fructose metabolism and the accompanying aerobic ATP formation were initiated only after fructose phosphorylation by the ATP derived from anaerobic breakdown of endogenous 3PGA. In contrast, addition of glucose started incorporation of 32P into acid-soluble compounds immediately after germination. In the latter case, NADH generated by glucose oxidation to gluconate (catalyzed by glucose dehydrogenase) might serve as an initial ATP source without depending on 3PGA breakdown and glucose metabolism via the Embden-Meyerhof pathway.

Adenosine Triphosphate↗
PubMed1979

Primary oxalosis: clinical and biochemical response to high-dose pyridoxine therapy.

Although pyridoxine hydrochloride (vitamin B6) is known to reduce the endogenous production of oxalate in some individuals with primary oxalosis, the dose for a satisfactory trial of treatment is not established. We report two cases of primary oxalosis on a daily regimen of 1 g pyridoxine hydrochloride, in which 24-hr urinary oxalate excretion decreased by 60% and 70%, respectively, with corresponding clinical benefit. The responses have been sustained up to 2.5 yr in one case, and 20 mo in the other. In the patient with renal failure, serum creatinine decreased from 243 to 146 mumole/liter after 15 mo of treatment. The decrease in glycollic acid excretion in both patients was consistent with an increase of glyoxalate transaminase activity by the vitamin. Supranormal levels of erythrocyte glutamic oxaloacetate transaminase (egot) activity were observed during therapy, and these may be useful as a measure of the effective dose of pyridoxine.

Adult↗
PubMed1997

Mechanism of inhibition of acid production in Streptococcus mutans by sodium ions under strictly anaerobic conditions.

Acids excreted and intracellular levels of glycolytic intermediates during glucose metabolism in streptococcus mutans NCTC 10449 under strictly anaerobic conditions were quantified in an attempt to understand the effect of sodium ions on bacterial acid production. In the presence of NaCl (0.15-0.30 M), the total amount of individual carboxylic acids excreted was inhibited by up to 31%. The intracellular level of fructose 1,6-bisphosphate increased by 58% and levels of 3-phosphoglycerate and pyruvate decreased by 46% and 12%, respectively. Sodium ions directly inhibited the activities of fructose 1,6-phosphate aldolase and triose phosphate isomerase. This indicated that the glycolytic enzymes responsible for the catalysis of fructose 1,6-bisphosphate to 3-phosphoglycerate were inhibited. However, in spite of the expected reduction in acid production intracellularly, the intracellular pH actually decreased in the presence of sodium ions. It is possible that the low intracellular pH inhibits the activity of the glycolytic enzymes involved in the breakdown of fructose 1,6-bisphosphate to 3-phosphoglycerate.

Anaerobiosis↗
PubMed1996

Structural and mechanistic studies of enolase.

The high-resolution structure of yeast enolase cocrystallized with its equilibrium mixture of substrate and product reveals the stereochemistry of substrate/product binding and therefore the groups responsible for acid/base catalysis and stabilization of the enolate intermediate. Expression and characterization of site-specific mutant forms of the enzyme have confirmed the roles of amino acid side chains in the catalysis of the first and second steps of the reaction. Coordination of both required magnesium ions to the carboxylate of the substrate/product indicates a role for these cations in stabilization of the intermediate.

Binding Sites↗
PubMed1978

Pathway of degradation of nitrilotriacetate by a Pseudomonas species.

The pathway of degradation of nitrilotriacetate (NTA) was determined by using cell-free extracts and a 35-fold purification of NTA monooxygenase. The first step in the breakdown was an oxidative cleavage of the tertiary amine by the monooxygenase to form the aldo acid, glyoxylate, and the secondary amine, iminodiacetate (IDA). NTA N-oxide acted as a substrate analog for induction of the monooxygenase and was slowly metabolized by the enzyme, but was not an intermediate in the pathway. No intermediate before IDA was found, but an unstable alpha-hydroxy-NTA intermediate was postulated. IDA did undergo cleavage in the presence of the purified monooxygenase to give glyoxylate and glycine, but was not metabolized in cell-free extracts. Glyoxylate was further metabolized by cell-free extracts to yield CO2 and glycerate or glycine, products also found from NTA metabolism. Of the three bacterial isolates in which the NTA pathway has been studied, two strains, one isolated from a British soil and ours from a Michigan soil, appear to be almost identical.

Acetates↗
PubMed1972

Observation of cooperative ionizations in hemoglobin.

(19)F-Nuclear magnetic resonance studies of specifically fluorinated hemoglobin derivatives have been used to determine the apparent pK(a) of the histidine beta146 imidazole in deoxyhemoglobin. The titration of this residue was found to be abnormally sharp, particularly in the presence of diphosphoglyceric acid. The explanation advanced for this unusual titration curve may have implications for the mechanism of cooperative ligand binding. The possible role of such ionizations is discussed in light of some chemical evidence that the cooperative binding process is governed to a greater extent by internal nonpolar forces than by electrostatic interactions of exposed groups.

Fluorine↗
PubMed2006

Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii.

The pathway for the synthesis of the organic solute glucosylglycerate (GG) is proposed based on the activities of the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP) from Methanococcoides burtonii. A mannosyl-3-phosphoglycerate phosphatase gene homologue (mpgP) was found in the genome of M. burtonii (http://www.jgi.doe.gov), but an mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) was absent. The gene upstream of the mpgP homologue encoded a putative glucosyltransferase that was expressed in Escherichia coli. The recombinant product had GpgS activity, catalyzing the synthesis of glucosyl-3-phosphoglycerate (GPG) from GDP-glucose and d-3-phosphoglycerate, with a high substrate specificity. The recombinant MpgP protein dephosphorylated GPG to GG and was also able to dephosphorylate mannosyl-3-phosphoglycerate (MPG) but no other substrate tested. Similar flexibilities in substrate specificity were confirmed in vitro for the MpgPs from Thermus thermophilus, Pyrococcus horikoshii, and "Dehalococcoides ethenogenes." GpgS had maximal activity at 50 degrees C. The maximal activity of GpgP was at 50 degrees C with GPG as the substrate and at 60 degrees C with MPG. Despite the similarity of the sugar donors GDP-glucose and GDP-mannose, the enzymes for the synthesis of GPG or MPG share no amino acid sequence identity, save for short motifs. However, the hydrolysis of GPG and MPG is carried out by phosphatases encoded by homologous genes and capable of using both substrates. To our knowledge, this is the first report of the elucidation of a biosynthetic pathway for glucosylglycerate.

Archaea↗
PubMed2001

Cutinase unfolding and stabilization by trehalose and mannosylglycerate.

The unfolding of cutinase at pH 4.5 was induced by increasing the temperature and guanidine hydrochloride concentration in the presence of potassium chloride, trehalose, and mannosylglycerate potassium salt. Protein thermal unfolding approached a two-state process, since the unfolding transitions were coincident within experimental error when assessed by near-ultraviolet (UV) difference, tryptophyl, and 8-anilino-1-naphthalene sulfonic acid (ANS) fluorescence spectroscopy. Trehalose at 0.5 M increased the temperature at which 50% of cutinase is unfolded by 3 degrees C. Unfolding induced by guanidine hydrochloride is clearly a non-two-state process. The presence of a stable intermediate was detected because unfolding assessed by near-UV difference spectroscopy occurs earlier than unfolding assessed by tryptophyl fluorescence. The intermediate is molten globule in character: the ANS fluorescence is higher than in the presence of the folded or unfolded state, showing native-like secondary structure and losing many tertiary interactions of the folded state, i.e., those surrounding the tyrosyl microenvironment. The stabilization effect of trehalose and mannosylglycerate was quantified by fitting the unfolding transitions to a model proposed by Staniforth et al. (Biochemistry 1993;32:3842-3851). This model takes into consideration the increase in solvation energies of the amino acid side-chains as the denaturant concentration was increased and the fraction of amino acid side-chains that become exposed in the unfolded structure of cutinase. Trehalose and mannosylglycerate stabilize the folded state relative to the intermediate by 1.4-1.6 and 1.6 kcal/mol and the intermediate relative to the unfolded state by 1.0 and 1.5 kcal/mol, respectively.

Carboxylic Ester Hydrolases↗
PubMed1987

The triose model: glyceraldehyde as a source of energy and monomers for prebiotic condensation reactions.

Glyceraldehyde acts as a source of energy and monomers in a new model of the origin of life. The simplest form of the model functions by converting formaldehyde from the environment into glyceraldehyde which spontaneously forms hemiacetal adducts that are oxidized to polyglyceric acid. Polyglyceric acid, in turn, acts as an autocatalyst with a rudimentary replicating ability. A unique property of the model is its ability to unite the origin of metabolism and the origin of polymer synthesis into a single process. Furthermore, the chemical resemblance of the model to glycolysis gives it the potential to develop a biological metabolism in a straightforward manner.

Calorimetry↗
PubMed1999

Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.

The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.

Binding Sites↗
PubMed1987

Identification of inositol hexaphosphate in 31P-NMR spectra of Dictyostelium discoideum amoebae. Relevance to intracellular pH determination.

A sugar phosphomonoester, myo-inositol hexakisphosphate (phytic acid), has been identified as a major phosphorylated metabolite in Dictyostelium discoideum amoeba. Its intracellular concentration was estimated to be 0.7 mM. The identification was made in perchloric acid extracts on the basis of 31P-NMR chemical shift values and their variations with pH, by addition of authentic compound and by hydrolysis with wheat phytase. Perchloric acid extracts were prepared so as to avoid losses of insoluble salts of polyphosphorylated compounds with divalent cations. The glycolytic intermediate, 3-phosphoglycerate accumulated intracellularly in amoebae incubated in the presence of fluoride. The pH sensitive NMR signal of 3-phosphoglycerate was used to monitor cytosolic pH and a value of pH 7.4 was found in aerobic Dictyostelium amoebae.

6-Phytase↗
PubMed1993

Urinary sugar phosphates and related organic acids in fructose-1,6-diphosphatase deficiency.

Two sisters with fructose-1,6-diphosphatase deficiency are reported. They presented with ketonuria, elevated plasma transaminase activity and severe metabolic acidosis during hypoglycaemic crises, which resembled Reye syndrome. Intravenous fructose tolerance tests provoked severe hypoglycaemia and metabolic acidosis. Fructose-1,6-diphosphatase activities in both peripheral leukocytes and cultured lymphocytes were below the limit of detection. Urinary organic acid analysis during crises revealed markedly increased excretion of lactate, ketone bodies, glycerol and glycerol-3-phosphate. We newly identified other glycolytic intermediates, glyceraldehyde, 3-phosphoglycerate and fructose-1,6-diphosphate, in the urine during hypoglycaemic attacks or after fructose tolerance tests. Identification of such compounds may be useful in the early diagnosis of this disease.

Female↗
PubMed1989

One- and two-dimensional NMR studies of yeast phosphoglycerate kinase.

One- and two-dimensional proton NMR studies have been carried out on yeast phosphoglycerate kinase (Mr approximately 45,000) in order to identify amino-acid spin systems and obtain sequence-specific assignments. A number of sequence-specific assignments have been made using a combination of structural information contained in nuclear Overhauser effect spectra and X-ray crystallographic data. The results of substrate binding studies (both 3-phosphoglycerate and Mg.ATP), which indicate mutual reorientation of certain assigned aromatic residues in the inter-domain region of the protein, are discussed.

Adenosine Triphosphate↗
PubMed1970

Mechanism of action of thyroid hormones on erythrocyte 2,3-diphosphoglyceric acid synthesis.

Normal erythrocytes, when incubated with thyroid hormone, were found to have increased levels of 2,3-diphosphoglyceric acid. In addition, a partially purified enzyme preparation, when incubated with either a 1,3-diphosphoglyceric acid generating system or 1,3-diphosphoglyceric acid directly, showed increased levels of 2,3-diphosphoglyceric acid when exposed to thyroid hormone. The hormonal effect was biphasic and was witnessed after 5 min of incubation. Substitution on the 3 and 5 positions of the basic thyronine molecule was essential for hormonal effect. It appears that thyroid hormone acts by directly stimulating the diphosphoglycerate mutase enzyme. The hormonal effect on 2,3-DPG synthesis may offer a biochemical explanation for the shift in the oxyhemoglobin dissociation curve observed in thyroid disorders.

Adenosine Triphosphate↗
PubMed1981

Preparation and physiological properties of alkyl esters of 2,3-dihydroxypropionic acid.

In order to investigate the physiological behavior of alkyl esters of 2,3-dihydroxypropionic acid two such compounds have been synthesized. One of them, the 1-dodecylester of 2,3-ditetradecyloxypropionic acid was subjected to digestion by pancreatic lipase. The substance remained unaffected. For an in vivo experiment a doubly labelled homolog, the [1'-14C]decyl ester of 2,3-di[1'-3H]hexadecyloxypropionic acid was synthesized. This compound was fed by stomach tube to three groups of male albino rats. The experimental animals were killed after 2,4 and 6 h, those of the control groups after 6 h. Blood, urine, small intestines and livers were examined for radioactivity. From the recovery rates it could be derived that the molecule had been metabolized and absorbed. Obviously, the alkyl chain labelled with 14C was split off first and the alkyl chains labelled with 3H were split off thereafter. As the substance is metabolized in vivo it cannot be utilized as a 'non-fattening fat'.

Animals↗
PubMed2006

Diversity and biosynthesis of compatible solutes in hyper/thermophiles.

The accumulation of compatible solutes, either by uptake from the medium or by de novo synthesis, is a general response of microorganisms to osmotic stress. The diversity of compatible solutes is large but falls into a few major chemical categories, such as carbohydrates or their derivatives and amino acids or their derivatives. This review deals with compatible solutes found in thermophilic or hyperthermophilic bacteria and archaea that have not been commonly identified in microorganisms growing at low and moderate temperatures. The response to NaCl stress of Thermus thermophilus is an example of how a thermophilic bacterium responds to osmotic stress by compatible solute accumulation. Emphasis is made on the pathways leading to the synthesis of mannosylglycerate and glucosylglycerate that have been recently elucidated in several hyper/thermophilic microorganisms. The role of compatible solutes in the thermoprotection of these fascinating microorganisms is also discussed.

Archaea↗