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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Quantitative analysis of the time courses of fluorescence anisotropy changes due to the binding of fructose-1,6-bisphosphate aldolase to the dissociable cytoplasmic glycerol-3-phosphate dehydrogenase covalently labelled with fluorescent dye was carried out. The behaviour of the aldolase-dehydrogenase system seems to be consistent with a cyclic reversible model characterized by the formation and dissociation of complexes of both the monomeric and the dimeric forms of dehydrogenase with aldolase, and rapid equilibrium between the free monomeric and dimeric forms of dehydrogenase. The half-life time of the formation of dimeric dehydrogenase-aldolase complex at the concentration of the enzymes expected to exist in the cell (i.e. in the micromolar range) is some minutes, and the time needed for equilibration between the aldolase-bound dimeric and monomeric forms of dehydrogenase is a few minutes as well. Consequently, one may expect that both the formation and the dissociation of this heterologous enzyme complex have physiological relevance.
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PMID:Kinetic pathways of formation and dissociation of the glycerol-3-phosphate dehydrogenase-fructose-1,6-bisphosphate aldolase complex. 403 65

1. Dihydroxyacetone phosphate exists in neutral aqueous solution at 20 degrees C as a mixture of keto, gem-diol and enolic forms in the ratio 55:44:1. 2. The three forms are freely interconvertible and rate constants for these reactions have been determined. 3. Keto-dihydroxyacetone phosphate is the primary reactive species in the reactions catalysed by alpha-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase. 4. The proportion of keto form to gem-diol forms of dihydroxyacetone phosphate is temperature-dependent. At 37 degrees C, 83% is keto-dihydroxyacetone phosphate. 5. The enzymological and metabolic consequences of these results are discussed.
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PMID:Dihydroxyacetone phosphate. Its structure and reactivity with -glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications. 433 Jan 97

Analogues of dihydroxyacetone phosphate and of 3-phosphoglycerate were made in which the phosphate group, -O-PO(3)H(2), is replaced by the phosphonomethyl group, -CH(2)-PO(3)H(2). The analogue of dihydroxyacetone phosphate is a substrate for aldolase and glycerol 1-phosphate dehydrogenase (Stribling, 1974), but not for triose phosphate isomerase. The analogue of 3-phosphoglycerate oxidizes NADH under the combined action of 3-phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase if ATP is added. Thus four out of the five glycolytic enzymes tested handle the phosphonomethyl compounds like the natural phosphates.
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PMID:Phosphonomethyl analogues of phosphate ester glycolytic intermediates. 437 3

The enzymic synthesis of the 1-phosphonomethyl isostere of fructose 1,6-diphosphate in which the 1-phosphate (-OPO(3)H(2)) is replaced by the phosphonomethyl group (-CH(2)PO(3)H(2)) is described. The kinetic properties of this fructose diphosphate isostere and of 4-hydroxy-3-oxobutylphosphonic acid, an isostere of dihydroxyacetone phosphate, with aldolase (EC 4.1.2.13), fructose diphosphatase (EC 3.1.3.11) and glycerol phosphate dehydrogenase (EC 1.1.1.8) are described (see Table 1).
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PMID:Properties of the phosphonomethyl isosteres of two phosphate ester glycolytic intermediates. 437 4

Pyridoxal phosphate can act as a specific photosensitizer for amino acid residues in rabbit muscle and spinach leaf aldolases, but the residues affected depend on the pH of the reaction. Below pH 8 one histidine residue per enzyme subunit is destroyed; above pH 8.5 there is little loss of histidine, and photoinactivation is associated with the destruction of specific tyrosine residues, particularly the COOH-terminal residues. Pyridoxal and 4-pyridinecarboxaldehyde are much less effective than pyridoxal phosphate at neutral pH, but are similar to pyridoxal phosphate in their photosensitizing activity at the higher pH. Compounds lacking the aldehyde group or the pyridine ring show little or no activity. A number of other enzymes, including alpha-glycerophosphate dehydrogenase, glucose-6-phosphate dehydrogenase, and yeast hexokinase, were also photoinactivated in the presence of pyridoxal phosphate; however, rabbit liver aldolase and two isomerases tested were completely resistant. The results suggest that certain enzymes, including rabbit muscle and spinach aldolases, but not rabbit liver aldolase, contain a specific site which interacts with pyridoxal phosphate, and that the conformation of this site changes in the pH range between 8.0 and 8.5
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PMID:Photoinactivation of aldolases by pyridoxal phosphate and its analogues. 527 95

A simple, continuous assay for aminoacyl-tRNA synthetases utilizing a commercially available pyrophosphate assay reagent kit was demonstrated. The method coupled aminoacyl-tRNA synthetase activity with pyrophosphate-dependent fructose-6-phosphate kinase, aldolase, triosephosphate isomerase, and glycerophosphate dehydrogenase. PPi formation was correlated with the oxidation of NADH, and was monitored continuously by the decrease of absorbance at 340 nm.
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PMID:Continuous spectrophotometric assay for aminoacyl-tRNA synthetases. 609 60

A method is presented for the simultaneous purification of hexokinase, fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase, and the partial purification of glycerol-3-phosphate dehydrogenase (NAD+), 6-phosphofructokinase, glucosephosphate isomerase, and glycerol kinase from Trypanosoma brucei. As a first step, the glycosomes, microbody-like organelles of Trypanosomatidae, containing almost exclusively enzymes involved in glucose and glycerol metabolism [Opperdoes, F. R. and Borst, P. (1977) FEBS Lett. 80, 360-364], were purified eightfold from homogenates with an average yield of 38%. Subsequently, the glycosomal content was subjected to hydrophobic interaction chromatography on phenyl-Sepharose. This step results in pure hexokinase (15% final yield) and almost pure triosephosphate isomerase, while the other glycosomal enzymes elute as mixtures of two or three enzymes. Triosephosphate isomerase was further purified to homogeneity on CM-cellulose (33% final yield), while phosphoglycerate kinase and fructose-bisphosphate aldolase were separated from each other and purified to homogeneity by affinity chromatography using ATP-Sepharose (25% and 30% final yields, respectively). Fructose-bisphosphate aldolase was further characterized as a typical class I enzyme.
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PMID:Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei. 648 38

A threefold decrease in specific activity of glycerol-3-phosphate dehydrogenase was found on going from 800 nM to 10 nM enzyme concentration. According to ultracentrifugal analyses the dimeric glycerol-3-phosphate dehydrogenase (molecular weight 78,000) dissociates into monomers in the equilibrium mixture of its substrates and products. The concentration-dependent decrease in the specific activity is interpreted as a consequence of subunit dissociation and the estimated dissociation constants are 0.7 micro M and 3.5 micro M at 38 degrees C and 20 degrees C respectively. According to active-enzyme-band centrifugation experiments and kinetic analysis aldolase forms a complex with glycerol-3-phosphate dehydrogenase and this complex formation influences the specific activity of the dehydrogenase. The interaction between glycerol-3-phosphate dehydrogenase and aldolase can provide a regulatory mechanism at the branching point of glycolytic and lipid metabolic pathways.
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PMID:Substrate-induced dissociation of glycerol-3-phosphate dehydrogenase and its complex formation with fructose-bisphosphate aldolase. 677 45

Changes in the activity of 13 enzymes are described in the process of cytodifferentiation of the nerve cells of spinal ganglion, the motor neurons of spinal cord and large nerve cells of the III layer of tectum opticum in 7, 10 and 21 day old chick embryos. Cytophotometry was performed with MZFV-1 (LOMO) by means of plug-method. A relatively high activity of glucose-6-phosphat dehydrogenase, diaphorase, alpha-glycerophosphate dehydrogenase and, partially, acetylcholine esterase was found already in the 7 days old embryo. The activity of monoamine oxidase, aldolase-glyceroaldehyde phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase increased markedly on the 21st day. When studying the reciprocal distribution of two enzymes in separate cells, pairs of enzymes with a high value of correlation coefficient were found. The cytodifferentiation was found to be accompanied by changes in the coefficient of correlation of the same pair of enzymes.
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PMID:[Enzymes in the process of neuronal differentiation of the hen spinal ganglion, spinal cord and tectum opticum. A cytophotometric histochemical study]. 683 47

In extracts of adult Angiostrongylus cantonensis, the activities of enzymes including glucokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, triosepho sphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglycerokinase, phosphoglyceromutase, enolase, pyruvate kinase, lactate dehydrogenase, pyruvate decarboxylase, alcohol dehydrogenase, glucose 6-phosphate dehydrogenase, glycerophosphate dehydrogenase and pyruvate dehydrogenase complex were demonstrated. The present of significant activity of glycerophosphate dehydrogenase and glucose 6-phosphate dehydrogenase may indicate the possibility of an operative of alpha-glycerophosphate and pentose phosphate pathway.
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PMID:Glycolytic enzymes in juvenile and adult Angiostrongylus cantonensis. 711 11


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