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 1,081 records · Page 60Linked to original sources
PubMed1983

Characterization of alpha alpha, beta beta, gamma gamma and alpha gamma human enolase isozymes, and preparation of hybrid enolases (alpha gamma, beta gamma and alpha beta) from homodimeric forms.

Four forms (alpha alpha, beta beta, gamma gamma and alpha gamma) of enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) were purified from human brain and skeletal muscle. Each purified preparation showed a single band on SDS-polyacrylamide gel electrophoresis, with a relative mobility corresponding to a molecular weight of about 46 000 for alpha and gamma subunits, or 44 000 for the beta subunit. The four enzymes showed similar values of specific activity (about 80 units/mg), optimal pH (pH 6.8-6.9), and Km for 2-phosphoglycerate (about 3 X 10(-5) M). Amino acid analysis, peptide mapping analysis with a limited proteolysis, and immunochemical studies of the purified enzymes revealed that the three subunits, alpha, beta and gamma, are distinct proteins. Three hybrid enolases (alpha gamma, beta gamma and alpha beta) could be prepared from a mixture of two homodimeric enolases by dissociation and reassociation procedures, followed by isolation with ion-exchange column chromatography.

Amino Acids↗
PubMed1989

Covalent cofactor binding to flavoenzymes requires specific effectors.

Modification by covalent FAD attachment to a histidine residue via an 8 alpha-(N3-histidyl)-riboflavin linkage occurs in several flavoenzymes. Among them is 6-hydroxy-D-nicotine oxidase (6-HDNO) of Arthrobacter oxidans and the flavoprotein subunits of the fumarate reductase and succinate dehydrogenase complex of Escherichia coli and other bacterial and eukaryotic cells. We found that 6-HDNO holoenzyme formation from apo-6-HDNO, monitored by [14C]FAD incorporation and increase in enzyme activity, can be mediated not only by phosphoenolpyruvate [Nagursky, H., Bichler, V. and Brandsch, R. (1988) Eur. J. Biochem. 177, 319-325], but also by one of the glycolytic intermediates glyceraldehyde-3-P, glycerate-3-P, or the intermediate in glycerol utilization by bacteria, glycerol-3-P. Apoflavoprotein of fumarate reductase and succinate dehydrogenase was obtained in an E. coli riboflavin-requiring strain (E. coli RR28rf) overexpressing the frdABCD or the sdhCDAB operon from the recombinant plasmids pGS39 and pGS141, respectively. In extracts obtained from these cells, flavoprotein flavinylation, analyzed as covalent [14C]FAD incorporation into the apoflavoprotein polypeptide by polyacrylamide gel electrophoresis and fluorography, was stimulated severalfold by the citric acid cycle intermediates citrate, isocitrate, succinate and fumarate. Our results suggest that covalent modification and thus activation of these enzymes is dependent on specific metabolic intermediates which may act as allosteric effectors in the reaction.

Citrates↗
PubMed1987

Studies on avian erythrocyte metabolism. XVI. Accumulation of 2,3-bisphosphoglycerate with shifts in oxygen affinity of chicken erythrocytes.

The ability of the chicken erythrocyte to accumulate 2,3-bisphosphoglycerate (2,3-P2-glycerate) and its effect upon the oxygen affinity (P50) of the cell suspensions have been determined. Erythrocytes from chick embryos, which contain 4-6 mM 2,3-P2-glycerate, and from chickens at various ages, which contain 3-4 mM inositol pentakisphosphate but no 2,3-P2-glycerate, were incubated with inosine, pyruvate, and inorganic phosphate. Red blood cells from 20-day chick embryos incubated in Krebs-Ringer, pH 7.45, containing 20 mM inosine and 20 mM pyruvate had an increase in 2,3-P2-glycerate from 4.3 to 11.9 mM after 4 h. Importantly, as 2,3-P2-glycerate concentration increased there was a corresponding increase in P50 of the cell suspension. Further, erythrocytes from 9- and 11-week, and 7-, 14-, 24-, and 28-month-old chickens when incubated similarly with inosine and pyruvate accumulated 2,3-P2-glycerate with corresponding increases in P50 of the cell suspensions. The ability of the red cell to accumulate this compound under the incubation conditions used apparently decreases with age of the bird (e.g., 11.9 mM in the 20-day embryo to 1.1 mM in the 28-month-old chicken after 4 h incubation). Despite the presence of significant amounts of inositol-P5, the accumulation of 2,3-P2-glycerate markedly decreases oxygen affinity of the cell suspensions. The delta P50/mumol increase in 2,3-P2-glycerate in the red cells of the 20-day chick embryo after 4 h incubation is 1.5 Torr; conversely, the delta P50/mumol decrease in 2,3-P2-glycerate in the red cells of the 17-day embryo after 6 h incubation in the presence of sodium bisulfite is 2.8 Torr. The demonstrated ability of the chicken erythrocyte to accumulate 2,3-P2-glycerate in response to certain substrates suggests that regulation of concentration of this compound could contribute significantly to regulation of blood oxygen affinity in birds.

2,3-Diphosphoglycerate↗
PubMed1997

Identification and mutation of a gene required for glycerate kinase activity from a facultative methylotroph, Methylobacterium extorquens AM1.

A gene (gckA) responsible for the activity of glycerate kinase has been identified within a chromosomal fragment of the serine cycle methylotroph Methylobacterium extorquens AM1. A mutation in gckA leads to a specific C1-negative phenotype. The polypeptide sequence derived from gckA showed high similarity to a product of ttuD essential for tartrate metabolism in Agrobacterium vitis. Our data suggest that gckA and ttuD might be structural genes for glycerate kinase and that the serine cycle and the tartrate utilization pathway share a series of reactions.

Base Sequence↗
PubMed2006

Restrictive cardiomyopathy in a patient with primary hyperoxaluria type II.

This is the first report of a cardiac manifestation of a primary hyperoxaluria type II (PH II) with the hemodynamic characteristics of a severe restrictive cardiomyopathy. PH II is a rare inherited metabolic disease characterized by a deficiency of D-glycerate dehydrogenase, which has also glyoxylate reductase activity. This defect causes an accumulation of hydroxypyruvate the precursor of oxalate. The renal excretion of oxalate is impaired causing a deposition of oxalate mainly in the kidneys. To date, less than fifty cases have been reported. Systemic oxalosis in PH II is an occasional finding; thus far, myocardial oxalosis due to PH II has never been reported. Described is the case of a 41 year old male with renal failure and severe neuropathy of unknown cause, who underwent endomyocardial biopsy under the suspicion of cardiac amyloidosis. Echocardiography and cardiac catheterization showed a severe restrictive cardiomyopathy; endomyocardial biopsy established the diagnosis of oxalosis. Plasma oxalate levels were markedly increased, therefore a liver biopsy was performed. Immunoreactivity for D-glycerate dehydrogenase/ glyoxylate reductase was absent and activity of the enzyme was < 5% of normal. In summary, these findings established the diagnosis of a restrictive cardiomyopathy due to PH II.

Adult↗
PubMed2006

The bifunctional glyceryl transferase/phosphatase OzmB belonging to the HAD superfamily that diverts 1,3-bisphosphoglycerate into polyketide biosynthesis.

The HAD superfamily protein OzmB from the oxazolomycin biosynthetic pathway is shown to divert the primary metabolite 1,3-diphosphoglycerate into the polyketide biosynthetic pathway as glycerate via loading of a carrier protein. Each of the steps-activation of d-3-phosphoglycerate, dephosphorylation while attached to a cysteine on OzmB, and subsequent transfer of glycerate to the phosphopantetheinyl thiol of an acyl carrier protein-was monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides.

Amino Acid Sequence↗
PubMedDate not supplied

[Carbon assimilation pathways in the methylotrophy of Pseudomonas gazotropha].

The dynamics of label distribution was studied in the products of 14CH3OH assimilation by the cells of Pseudomonas gazotropha Z-1156. Substances to be first detected were glycolate, glycine and those of the chromatogram "start" spot. Later, the radioactivity was detected in phosphorylated compounds and glycerate. Cell extracts of Ps. gazotropha Z-1156 contained ribosephosphate isomerase, phosphoribulokinase and glyceraldehyde dehydrogenase but not ribulosediphosphate carboxylase. Distribution of the label in the products of 14CH3OH assimilation and the presence of active hydroxypyruvate reductase in the extract suggest that the serine cycle is involved in methylotrophy of Ps. gazotropha Z-1156. This suggestion is confirmed by the presence of active formate dehydrogenase, phosphoenolpyruvate carboxylase, (NADP+, Mn2+)-specific isocitrate dehydrogenase, (NAD, Mg2+)-specific malate dehydrogenase, malate lyase, and isocitrate lyase. The citric acid cycle is open at the alpha-ketoglutarate dehydrogenase system. The dry biomass of Ps. gazotropha Z-1156 contains over 70% of protein.

Carbon↗
PubMed1988

Complex of brain D-phosphoglycerate mutase and gamma enolase and its reactivation by D-glycerate 2,3-bisphosphate.

The dissociabilities of dimeric gamma enolase, alpha enolase, and phosphoglycerate mutase of brain origin were tested using fluorescein isothiocyanate attached covalently to these enzymes. The dissociation constant of dimeric gamma enolase is lower (Kd = 0.03 microM) than that of the alpha enolase (Kd = 3 microM), while dimeric mutase seems to be nondissociable in the concentration range 0.1-10 microM, at pH 7.3 in 50 mM imidazole buffer at 20 degrees C. Interaction of neuron-specific gamma enolase with D-phosphoglycerate mutase was detected with the same fluorescence-labeling technique as well as by a kinetic analysis. The determined dissociation constant of the enolase-mutase complex was found to be in the range 5-40 microM, independent of the technique used. A mixed type of inhibition in the binding of D-glycerate-2-P and mutase to the D-glycerate-2-P binding site on enolase was observed in the absence of D-glycerate-2,3-P2. However, the inhibition of the enolase activity by brain D-phosphoglycerate mutase in the D-glycerate-2-P----phosphoenolpyruvate transformation is almost fully reverted by D-glycerate-2,3-P2, probably via the proper coordination of the active centers in the ternary complex of enolase, D-phosphoglycerate mutase, and their common intermediate, D-glycerate-2-P. The mechanism of intermediate transfer by consecutive enzyme pairs in a nondivergent metabolite flux (around the transformation of D-glycerate-2-P) is examined and conclusions of the present experiments are compared with the results of an extended analysis performed earlier with a divergent metabolite flux (around the transformation of multiusage triosephosphates, D-glyceraldehyde-3-P, and dihydroxyacetone phosphate).

2,3-Diphosphoglycerate↗
PubMed1975

A specific enzyme for glucose 1,6-bisphosphate synthesis.

The reaction: glycerate-1,3-P2 PLUS GLUCOSE-1-P YIELDS TO GLUCOSE-1,6-P2 plus glycerate-P is catalyzed by a distinct enzyme of mouse brain. A divalent metal requirement was shown when the enzyme was treated with imidazole and EDTA. Mg2+, Mn2+, Ca2+, Zn2+, Ni2+, Co2+, and Cd2+ were quite effective cofactors. The enzyme, in better than 50 percent yield, has been purified away from 99 percent of the phosphoglucomutase, phosphoglycrate mutase, and phosphofructokinase. Acetyl-P, ATP, enolpyruvate-P, creatine-P, and fructose-1,6-P2 are not phosphoryl donors. Glucose-6-P and mannose-1-P are good alternate acceptors. Mannose-6-P, galactose-Ps, and fructose-Ps have little or no acceptor activity. Strong inhibition was found with fructose-1,6-P2, glycerate-2,3-P2, enolpyruvate-P, and acetyl CoA. From the amount of activity and the kinetic constants of the purified enzyme it seems likely that this enzyme is responsible for the glucose-1,6-P2 synthesis of brain.

Acetyl Coenzyme A↗
PubMed1980

Shift of the equilibrium constant of the 3-P-glycerate kinase reaction towards 1,3-bis-P-glycerate with adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) as substrate.

It has been demonstrated that the reaction of ATP beta S and 3-P-glycerate catalyzed by 3-P-glycerate kinase, unlike the reaction with ATP, can form a readily detectable amount of 1,3-bis-P-glycerate as observed by 31P NMR. By quantifying production of 1,3-bis-P-glycerate from the phosphorothioate analogue of ATP as a function of time as the reaction approaches equilibrium, Keq for the reaction was estimated to be approximately 400, about 1 order of magnitude less than the equilibrium constant previously reported for the analogous reaction of the normal nucleotide substrates.

Adenosine Triphosphate↗
PubMed1983

Fructose, fructose 1-phosphate, and glyceraldehyde breakdown in carbohydrate metabolism.

Recent investigations showed that all enzymes that are involved in the catabolism of fructose via fructose 1-phosphate (F-1-p) are present in the bovine lens. The present studies were performed to provide information regarding the extent to which fructose, F-1-p and glyceraldehyde (GA) are actually catabolized via this pathway, and how they increase the lactate, alpha-glycerophosphate and glycerol concentrations. Incubation was performed with a homogenate of bovine lens equator. F-1-p, and particularly fructose + ATP, considerably increased lactate and alpha-glycerophosphate concentrations, while the glycerol concentration remained unchanged compared to controls. Lactate formation through GA was not observed; while small amounts of glycerol and alpha-glycerophosphate are formed, it seems that the major part is transformed to glycerate. The results show that the further breakdown of lenticular fructose occurs via F-1-p and that the phosphorylated C3 fragments (dihydroxyacetone phosphate) are transferred to the energy metabolism, which is not the case with GA.

Animals↗
PubMed1982

Metabolism of l-Threonic Acid in Rumex x acutus L. and Pelargonium crispum (L.) L'Hér.

l-Threonic acid is a natural constituent in leaves of Pelargonium crispum (L.) L'Hér (lemon geranium) and Rumex x acutus L. (sorrel). In both species, l-[(14)C]threonate is formed after feeding l-[U-(14)C]ascorbic acid to detached leaves. R. acutus leaves labeled with l-[4-(3)H]- or l-[6-(3)H]ascorbic acid produce l-[(3)H]threonate, in the first case internally labeled and in the second case confined to the hydroxymethyl group. These results are consistent with the formation of l-threonate from carbons three through six of l-ascorbic acid. Detached leaves of P. crispum oxidize l-[U-(14)C] threonate to l-[(14)C]tartrate whereas leaves of R. acutus produce negligible tartrate and the bulk of the (14)C appears in (14)CO(2), [(14)C]sucrose, and other products of carbohydrate metabolism. R. acutus leaves that are labeled with l-[U-(14)C]threonate release (14)CO(2) at linear rate until a limiting value of 25% of the total [U-(14)C]threonate is metabolized. A small quantity of [(14)C]glycerate is also produced which suggests a process involving decarboxylation of l-[U-(14)C]threonate.

Journal Article↗
PubMed1971

Photosynthetic products of division synchronized cultures of euglena.

Rates and products of photosynthetic (14)CO(2) fixation by division synchronized cultures of Euglena gracilis strain Z were determined over the cycle. Rate of (14)CO(2) fixation doubled in a continuous manner throughout the light phase followed by a slight reduction of photosynthetic capacity in the dark phase. Greater (14)C incorporation into the nucleic acid-polysaccharide fraction occurred with mature cells. Products of (14)CO(2) fixation varied markedly over the cycle: although with mature cells (14)C-labeled sucrose was not detected, with dividing cells this was the main sugar labeled; in young cells (14)C maltose was formed. Cells removed at end of dark phase accumulated (14)C in glycolate, whereas at other stages over the cycle less (14)C was present in glycolate, and this was accompanied by a rapid incorporation of (14)C into glycine and serine. Glycerate was an early and major product of photosynthesis with cells at the mature stage of the cycle.Changes in ribulose 1,5-diphosphate carboxylase activity paralleled changes in photosynthetic rate, but activity was not great enough to account for the observed rates of CO(2) fixation at most stages of the division cycle investigated.

Journal Article↗
PubMed2000

Novel beta -hydroxyacid dehydrogenases in Escherichia coli and Haemophilus influenzae.

Our laboratory has previously reported a structurally and mechanistically related family of beta-hydroxyacid dehydrogenases with significant homology to beta-hydroxyisobutyrate dehydrogenase. A large number of the members of this family are hypothetical proteins of bacterial origin with unknown identity in terms of their substrate specificities and metabolic roles. The Escherichia coli beta-hydroxyacid dehydrogenase homologue corresponding to the locus was cloned and expressed with a 6-histidine tag for specific purification. The purified recombinant protein very specifically catalyzed the NAD(+)-dependent oxidation of d-glycerate and the NADH-dependent reduction of tartronate semialdehyde, identifying this protein as a tartronate semialdehyde reductase. Further evidence for identification as tartronate semialdehyde reductase is the observation that the coding region for this protein is directly preceded by genes coding for hydroxypyruvate isomerase and glyoxylate carboligase, two enzymes that synthesize tartronate semialdehyde, producing an operon clearly designed for d-glycerate biosynthesis from tartronate semialdehyde. The single beta-hydroxyacid dehydrogenase homologue from Haemophilus influenzae was also cloned, expressed, and purified with a 6-histidine tag. This protein also catalyzed the NAD(+)-dependent oxidation of d-glycerate but was significantly more efficient in the oxidation of four-carbon beta-hydroxyacids like d-hydroxybutyrate and d-threonine. This enzyme differs from all the presently known beta-hydroxybutyrate dehydrogenases which are well established members of the short chain dehydrogenase/reductase superfamily.

Alcohol Oxidoreductases↗
PubMed1977

Effects of bilirubin on red cell metabolism.

Blirubin causes certain defects in erythrocyte metabolism, mainly in glycolysis. These effects of bilirubin were studied in vitro using a relatively physiological assay medium, which consisted of heparinized whole blood. Bilirubin was added in a small quantity of NaOH solution. In the presence of bilirubin a reduced glucose consumption of red cells and an accelerated depletion in the ATP and glycerate-2,3-bisphosphate concentration was found. Bilirubin levels lower than 50 mumol/l did not influence the glucose consumption. In agreement to other investigations it was established that bilirubin causes haemolysis of red cells. ATP-deficient cells are more sensitive to this effect.

Adenosine Triphosphate↗
PubMed1982

The effect of aging on rat liver phosphoglycerate kinase and comparison with the muscle enzyme.

Pure liver phosphoglycerate kinase (ATP:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.2.3) from old rats has been found to be an altered enzyme with certain properties which are dissimilar to those of the enzyme obtained from young animals. Stability during storage, sensitivity to heat, response to antiserum and stability during isoelectric focusing differ. Unchanged are molecular weight, specific activity, Km, reactivity of SH groups, blocked N-terminal residue and leucine for the C-terminal residue. Liver phosphoglycerate kinase differs substantially from the muscle enzyme. Among the differences are stability, heat-sensitivity, Km for 3-phosphoglyceric acid, inactivation by urea and response to antiserum. Nonetheless, a number of properties suggest that the liver and muscle enzymes are similar in structure. Both react with antisera prepared to phosphoglycerate kinase from muscle and liver, respectively. For both enzymes, the N-terminal residue is blocked and the C-terminal amino acid is leucine. The muscle form has been named phosphoglycerate kinase-1 or A. The only previously known isozyme is the testis enzyme, phosphoglycerate kinase-2 or B. We therefore propose that the liver enzyme be known as phosphoglycerate kinase-3 or C.

Aging↗
PubMed1977

The effects of calcium on glycolysis and ATP concentration in complete and membrane-poor hemolyzates of human erythrocytes.

Hemolyzates prepared from packed human red cells with 30 micrometer total calcium were employed as a means to examine the relationship between ATP consumption and lactate formation. Hemolyzates exposed to ultracentrifugation accumulate membrane fragments in the top layer yielding membrane-poor fractions in the buttom layers of the centrifuge tube. Lactate formation accompanied by ATP depletion amounts to 12 mumoles per ml and hour in complete hemolyzates fortified with NAD. Complexation of calcium results in about 50% inhibition of the lactate formation with a concomitant increase of ATP. Lactate formation is reduced in membrane-poor hemolyzates approximately concurrently to the extent of membrance removal which produces no discernible change in the glyceral-dehydephosphate dehydrogenase activity. 50--200 micrometer total calcium has no effect on the membrane-independent lactate formation which amounts to 1--2 mumoles per ml and hour. Triton X-100 seems to solubilise also the membrane components responsible for the high calcium-dependent ATP consumption which governs the lactate formation.

Adenosine Triphosphate↗
PubMed1979

The breakdown of 2,3-bis(phospho)-D-glycerate by Fe(III)-haemoglobin.

Fe(III)-haemoglobin is shown to catalyse the hydrolysis of 2,3-bis(phospho)-D-glycerate to Pi and 3-phosphoglycerate, although the rate is slow, even when the protein is present at concentrations in the millimolar range. The rate of hydrolysis is proportional to the subtrate concentration up to at least 10 mM, so if the process is enzymic, the Km must be high.

Diphosphoglyceric Acids↗