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At least 883 records · Page 49Linked to original sources
PubMed1982

Cerebrospinal fluid aldolase, lactate and creatine phosphokinase in the differential diagnosis of meningitis and meningo-encephalitis.

Creatine phosphokinase, aldolase and lactate determinations were performed on serum and cerebrospinal fluid to assess their value in the diagnosis of tuberculous and purulent meningitis and meningo-encephalitis. Changes in serum were independent of those in the cerebrospinal fluid. Variable results for cerebrospinal fluid creatine phosphokinase were obtained in the three groups. Lactate concentrations in the cerebrospinal fluid showed a clear distinction between tuberculous meningitis and meningo-encephalitis with levels 5 mmol/1 highly suggesting tuberculous meningitis. Also elevated cerebrospinal fluid aldolase levels may exclude meningo-encephalitis as a likely diagnosis.

Adolescent↗
PubMedDate not supplied

[Amino acid composition and subunit structure of rabbit muscle aldolase in experimental atherosclerosis].

Under atherosclerosis the fractions corresponding to alpha-subunits are focused at a more alkaline pH than the same fractions in the norm. The curve of the enzymic activity of the fractions with atherosclerosis is higher. beta-subunits of aldolase from muscles of intact rabbits and those with sclerosis are identical in the amino acidic composition. In the enzyme alpha-subunits under conditions of atherosclerosis the content of lysine, serine, glycine, valine gets higher. On the basis of the previous research which reveals peptide having no analogs in the norm in the C-terminal fragment of aldolase molecule an assumption is advanced that under conditions of atherosclerosis the intermediate C-terminal site of the enzyme alpha-chain changes.

Amino Acids↗
PubMedDate not supplied

Studies on the interaction of fructose 1,6-P2 aldolase with methylglyoxal.

Reaction of rabbit muscle fructose 1,6-P2 aldolase with methylglyoxal results in a biphasic loss of activity. The kinetics of the initial rapid phase are first order with respect to the inhibitor. Dihydroxyacetone phosphate and fructose 1,6 bisphosphate afford complete protection whereas inorganic phosphate provides only a partial protection against inactivation. The treatment with methylglyoxal modifies the aldolase ability to bind D-Ga3P and DHAP. Loss of activity correlates with the modification of 1.7 arginine residues but data suggest that probably one of these arginine residues is essential. A likely role of this residue could be its interaction with the C1 negatively charged phosphate binding site of the enzyme.

Aldehydes↗
PubMedDate not supplied

Some evidence in favour of the partnership between rabbit muscle aldolase and glyceraldehyde 3-phosphate dehydrogenase in the consecutive reactions.

An additional indication in favour of interaction between sequential glycolytic enzymes is provided by the mutual enhancement of aldolase and glyceraldehyde 3-phosphate dehydrogenase activities. The efficiency of aldolase as the activator is progressively affected by the presence of its substrate, fructose-1,6-diphosphate, and its structural analogue, hexitol-1,6-diphosphate. Such interrelation of two sequential glycolytic enzymes can originate from their conformational interadjustment for the subsequent metabolic channeling between them.

Animals↗
PubMed1975

Cross-linking and coupling of rabbit muscle aldolase and glyceraldehyde-3-phosphate dehydrogenase by glutaraldehyde.

The mode of cross-linking of rabbit-muscle aldolase and glyceraldehyde-3-phosphate dehydrogenase by glutaraldehyde was studied. The about 5 A long reagent can partly cross-link subunits within the tetramers, whereas it is readily able to make intermolecular cross-links producing polymeric enzyme species. Of the two enzymes, glyceraldehyde-3-phosphate dehydrogenase has a greater tendency to polymerize in the presence of glutaraldehyde. In the case of aldolase, the inter- and intramolecular cross-links between subunits can be distinguished by SDS gel-electrophoresis. The copolymerization pattern of the two enzymes indicates that, though the formation of mixed polyenzymes can be detected by affinity chromatography on human erythrocyte ghosts, under the conditions tested these proteins do not form heterologous enzyme complexes that could be trapped by glutaraldehyde.

Aldehydes↗
PubMed1975

Synthesis and degradation of fructose diphosphate aldolase isoenzymes in avian brain.

The intraccellular proteins of animal cells are continuously turning over; therefore, the concentration of a given protein is regulated both at the level of protein synthesis and at the level of protein degradation. Studies on the relative rates of turnover of isoenzymes, such as those of aldolase and lactate dehydrogenase, may help to clarify the mechanisms involved in protein turnover. The isoenzymes and subunit types are very similar proteins, and are located within the same intracellular compartments; yet, the concentrations of these proteins are independently regulated. The present paper describes the roles of synthesis and degradation in regulating aldolase isoenzyme concentrations in avian brain...

Animals↗
PubMedDate not supplied

[Changes in the kinetic properties of aldolase and lactate dehydrogenase in the brain cytoplasm of mice following chronic gamma irradiation at low doses].

The effect of chronic low-dose (0.6 rad/day) 137Cs gamma-irradiation of mice was studied. It was shown that radiation causes changes in the kinetic parameters (Vmax, KM, Vmax/KM) and isoenzyme patterns of aldolase and lactate dehydrogenase of the brain cytoplasm of mice. The kinetic properties of both enzymes changes in 1, 2, 4 and 9 days after irradiation. The character of changes in Vmax of these enzymes depends on the original Vmax values. The level of the predominant LDH1 (H4) form increases while that of the specific tissular form (C4) decreases (acute on the 9th day). Different levels of sensitivity of aldolase, LDH, and their isoenzymes to low-doses of low-rate gamma-irradiation were observed.

Animals↗
PubMed1977

[Changes in aldolase and creatine kinase activity during thermal muscle damage].

A study was made of changes in outflux, extractability and enzyme (aldolase and creatine kinase) activity of muscle proteins induced by thermal action in skeletal muscles of R. temporaria L. Under a 15-minutes action of temperatures under 36 degrees C, which do not produce any contracture or fall of excitability, changes in a fraction of protein outfluxed from muscles were observed. The thermal action accompanied by the fall and irreversible loss of excitability (above 36 degrees) resulted in the fall of extractability and enzyme activity of water-soluble proteins extracted from homogenized muscles in addition to prolonged changes in the fraction of outfluxed proteins. The increased binding of aldolase by actomyosin under thermal injury of muscle is established. Changes of outflux extractability and enzyme activity of proteins during the thermal alteration of muscle are considered with regard to data about the complexing of muscle proteins.

Animals↗
PubMed1996

Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.

The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.

Aldehyde-Lyases↗
PubMed1990

In vitro expression of Lac-PTS and tagatose 1,6-bisphosphate aldolase genes from Lactococcus lactis subsp. cremoris plasmid pDI-21.

A 4.4-kb EcoR1-EcoR1 DNA fragment from the Lactococcus lactis subsp. cremoris plasmid pDI-21 encoded the tagatose 1,6-bisphosphate (TBP) aldolase gene and the Lac-PTS genes. In vitro transcription-translation using Escherichia coli S30 extract showed the synthesis of 41,000-, 23,000- and 12,000-dalton proteins which correspond to the TBP-aldolase, Lac-PTS enzyme II, and factor III proteins respectively.

Aldehyde-Lyases↗
PubMed2006

Aldolase C/zebrin II is released to the extracellular space after stroke and inhibits the network activity of cortical neurons.

Cell death after stroke involves apoptotic, autophagocytic and necrotic mechanisms which may cause the release of cytosolic proteins to the extracellular space. Aldolase C (AldC) is the brain specific isoform of the glycolytic enzyme fructose-1,6-bisphosphate aldolase. According to its characteristic striped expression pattern in the adult cerebellum AldC is also termed zebrin II. Here, we demonstrate release of AldC into the cerebrospinal fluid (CSF) after stroke in vivo. Studies with cell cultures confirmed that AldC is released to the extracellular space after hypoxia. Moreover, addition of purified recombinant AldC to networks of cortical neurons plated on multielectrode arrays reversibly inhibited the spontaneous generation of action potentials at AldC concentrations which can be expected to occur after lesions of the human cerebral cortex. This mechanism could be relevant in the pathogenesis of the electrophysiological changes in the penumbra region after stroke.

Adult↗
PubMed1986

Regulation of rat liver 4-hydroxy-2-ketoglutarate aldolase.

The possibility is examined that 4-hydroxy-2-ketoglutarate aldolase (4-hydroxy-2-ketoglutarate glyoxylatelyase, EC 4.1.3.16), the last step in hydroxyproline catabolism is regulated by intermediates of gluconeogenesis. Inhibition of isolated 4-hydoxy-2-ketoglutarate aldolase was examined using dual inhibition studies. It was found that the enzyme exhibits synergistic inhibition by oxaloacetate and pyruvate, but only when the substrate concentration is low. At substrate concentrations approaching saturation, the inhibition by the oxaloacetate and pyruvate becomes additive. These results are discussed in terms of possible control of the use of carbon from hydroxyproline breakdown in glucose production.

Animals↗
PubMed1992

Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.

Deoxyribose 5-phosphate aldolase was purified 41 times from Bacillus cereus induced by growth on deoxyribonucleosides. The purification procedure includes ammonium sulphate fractionation, gel filtration on Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel and preparative electrophoresis on 10% polyacrylamide gel. The enzyme is stable above pH 6.5, but is rapidly inactivated by sulfhydryl reagents. Being insensitive to EDTA, it may be considered as a Class I aldolase. Among a number of compounds tested (including some carboxylic acids, free and phosphorylated pentoses, nucleotides and nucleosides), none has been found to affect the enzyme activity. The enzyme appears to be dimeric, with a subunit Mr of 23,600. A Km of 4.4 x 10(-4) M was calculated for dRib 5-P.

Aldehyde-Lyases↗
PubMed1982

Comparative and developmental studies on 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase.

1. In rats, liver 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase activities are maximal in the suckling period. 2. Liver activities for 4-hydroxy-2-oxoglutarate aldolase, alanine-glyoxylate aminotransferase, serine-pyruvate aminotransferase and serine dehydratase, but not hydroxyproline oxidase, are increased in rats on a high-fat, carbohydrate-free diet. 3. It is suggested that 4-hydroxy-2-oxoglutarate may be a significant source of glyoxylate for glycine and hence glucose formation. 4. Mammalian liver hydroxyproline oxidase activity is higher in carnivorous species; necessary, perhaps, to metabolise a relatively large influx of hydroxyproline on a flesh diet.

Aging↗
PubMed2006

Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli.

MhpE (4-hydroxy-2-ketovalerate aldolase) and MhpF [acetaldehyde dehydrogenase (acylating)] are responsible for the last two reactions in the 3-(3-hydroxyphenyl)propionate (3-HPP) catabolic pathway in Escherichia coli, which is homologous to the meta-cleavage pathway in Pseudomonas species. Here, we report that the MhpE aldolase is associated with the MhpF dehydrogenase and that MhpF is indispensable for the folding of MhpE. Moreover, our results suggest that the mhpF and mhpE genes are translationally coupled through a reinitiation mechanism. This reinitiation mechanism may function in ensuring that the expression of mhpE occurs only when MhpF is available for the formation of a complex.

Aldehyde Oxidoreductases↗
PubMed2002

Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family.

Fructose-6-phosphate aldolase from Escherichia coli is a member of a small enzyme subfamily (MipB/TalC family) that belongs to the class I aldolases. The three-dimensional structure of this enzyme has been determined at 1.93 A resolution by single isomorphous replacement and tenfold non-crystallographic symmetry averaging and refined to an R-factor of 19.9% (R(free) 21.3%). The subunit folds into an alpha/beta barrel, with the catalytic lysine residue on barrel strand beta 4. It is very similar in overall structure to that of bacterial and mammalian transaldolases, although more compact due to extensive deletions of additional secondary structural elements. The enzyme forms a decamer of identical subunits with point group symmetry 52. Five subunits are arranged as a pentamer, and two ring-like pentamers pack like a doughnut to form the decamer. A major interaction within the pentamer is through the C-terminal helix from one monomer, which runs across the active site of the neighbouring subunit. In classical transaldolases, this helix folds back and covers the active site of the same subunit and is involved in dimer formation. The inter-subunit helix swapping appears to be a major determinant for the formation of pentamers rather than dimers while at the same time preserving importing interactions of this helix with the active site of the enzyme. The active site lysine residue is covalently modified, by forming a carbinolamine with glyceraldehyde from the crystallisation mixture. The catalytic machinery is very similar to that of transaldolase, which together with the overall structural similarity suggests that enzymes of the MipB/TALC subfamily are evolutionary related to the transaldolase family.

Aldehyde-Lyases↗
PubMed2000

Differential expression of plastidic aldolase genes in Nicotiana plants under salt stress.

Two homologous genes of plastidic fructose-1,6-bisphosphate aldolase (AldP) isozymes were isolated from green leaves of a salt stress-tolerant Nicotiana species, Nicotiana paniculata, by differential screening. The products of the corresponding genes, NpAldP1 and NpAldP2, were 91% identical to each other and 70-85% identical to the other known plant plastidic aldolases. Although these two genes showed similar organ-specific expression and daily cycles, their responses to salt stress differed: mRNA accumulation of NpAldP2 increased, but that of NpAldP1 slightly decreased. The mRNA accumulations of their counterparts of two other Nicotiana species, NeAldP1 and NeAldP2 (Nicotiana excelsior), and NaAldP1 and NaAldP2 (Nicotiana arentsii) were studied under the same stress condition. N. arentsii conserved accumulation profiles similar to N. paniculata, but N. excelsior did not. In N. excelsior, accumulation of NeAldP1 decreased to 50% of the control after stress and gradually recovered thereafter, whereas accumulation of NeAldP2 temporarily decreased and reached 250% of the control by the third day of stress. Southern blot analysis indicated that NpAldP1, NpAldP2, NaAldP1, and NaAldP2 include one or two closely related genes and NeAldP1 and NeAldP2 several.

Journal Article↗
PubMed2002

Cloning, isolation and characterization of the Thermotoga maritima KDPG aldolase.

The Thermotoga maritima aldolase gene has been cloned into a T7 expression vector and overexpressed in Escherichia coli. The preparation yields 470 UL(-1) of enzyme at a specific activity of 9.4 U mg(-1). During retroaldol cleavage of KDPG, the enzyme shows a k(cat) that decreases with decreasing temperature. A more than offsetting decrease in K(m) yields an enzyme that is more efficient at 40 degrees C than at 70 degrees C. The substrate specificity of the enzyme was evaluated in the synthetic direction with a range of aldehyde substrates. Although the protein shows considerable structural homology to KDPG aldolases from mesophilic sources, significant differences in substrate specificity exist. A preparative scale reaction between 2-pyridine carboxaldehyde and pyruvate provided product of the same absolute configuration as mesophilic enzymes, but with diminished stereoselectivity.

Aldehyde-Lyases↗