Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The activities of six enzymes (hexokinase, phosphoglucose isomerase, phosphofructokinase, aldolase, glucose 6-phosphate dehydrogenase and amylase) in extracts of pea cotyledons were determined. The activities during the first 10 days after germination showed individual and characteristic changes that indicate a specific control of both synthesis and destruction of enzymes. 2. Tissue contents of glucose, inorganic phosphate, glucose 6-phosphate, fructose 6-phosphate, ATP, ADP, AMP, NAD and NADP were also determined, and a correlation is reported between the substrate concentrations at day 1 and the subsequent enzymic activity. 3. The initial NAD(+)/NADH ratio value of 1 changed to about 3 by day 4; the NADP content was lower and changes in the oxidation state were less striking. The ratio of ATP to ADP and AMP remained virtually constant.
 ...
PMID:Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue during germination. 438 39

Genes for three enzymes of intermediary sugar metabolism in E. coli, zwf (glucose 6-phosphate dehydrogenase, constitutive), edd (gluconate 6-phosphate dehydrase, inducible), and eda (2-keto-3-deoxygluconate 6-phosphate aldolase, differently inducible) are closely linked on the E. coli genetic map, the overall gene order being man... old... eda. edd. zwf... cheB... uvrC... his. One class of apparent revertants of an eda mutant strain contains a secondary mutation in edd, and some of these mutations are deletions extending into zwf. We have used a series of spontaneous edd-zwf deletions to map a series of point mutants in zwf and thus report the first fine structure map of a gene for a constitutive enzyme (zwf).
 ...
PMID:Deletion mapping of zwf, the gene for a constitutive enzyme, glucose 6-phosphate dehydrogenase in Escherichia coli. 456 65

1. The degradation rates and half-lives of hexokinase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase, pyruvate kinase, glucose 6-phosphate dehydrogenase, phosphoglycerate kinase and aldolase were calculated from measurements of the decline in activities of these enzymes in rat small intestine during starvation. 2. The half-lives of the enzymes are: hexokinase, 5.7h; 6-phosphogluconate dehydrogenase, 7.6h; glucose 6-phosphate dehydrogenase, 6.0h; pyruvate kinase, 8.9h; lactate dehydrogenase, 8.7h; phosphoglycerate kinase, 8.7h; aldolase, 5.1h. 3. The significance of the results is discussed with respect to the regulation of enzyme concentrations in response to changes in diet.
 ...
PMID:Degradation of glucose-metabolizing enzymes in the rat small intestine during starvation. 472 2

Spirillum itersonii ATCC 12639 utilized d-fructose but neither d-glucose nor d-gluconate as a sole source of carbon and energy. The substrate saturation kinetics for d-fructose and d-glucose uptake by whole cells indicated the presence of a carrier-mediated transport system for d-fructose but not for d-glucose. The d-fructose uptake activity was induced (10- to 12-fold increase) during growth on d-fructose-Casamino Acids (CA) or d-glucose-CA medium, but not CA alone. d-Fructose uptake activity was stimulated by Na(+) or Li(+), but was inhibited by KCN, NaN(3), 2,4-dinitrophenol, and p-chloromercuribenzoate. High specific activities of glucokinase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydratase, and 2-keto-3-deoxy-6-phosphogluconate aldolase were detected in extracts of cells cultured on d-fructose-CA medium. These enzymatic activities were undetectable in extracts of cells grown in CA or succinate-CA medium. No decrease in the maximally induced specific activities of these enzymes occurred after the addition of succinate to cells during exponential growth on d-fructose-CA. Fructose 1,6-diphosphate aldolase and glucose-6-phosphate isomerase specific activities were approximately the same irrespective of cultural conditions. These results indicated that d-glucose was not utilized by cells of S. itersonii because this bacterium was impermeable to this hexose.
 ...
PMID:Transport and catabolism of D-fructose by Spirillum itersomii. 480 97

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
 ...
PMID:Photoinactivation of aldolases by pyridoxal phosphate and its analogues. 527 95

1. The products of the lactoperoxidase-catalysed oxidation of thiocyanate by hydrogen peroxide were sulphate, carbon dioxide and ammonia. Cyanate, sulphite and a compound showing increased extinction at 235mmu (the ;235 compound') were intermediate oxidation products. 2. Two of the intermediates acted as electron acceptors in the oxidation of NADH(2). Thus NADH(2) was oxidized by sulphite in the presence of lactoperoxidase (EC 1.11.1.7) and Mn(2+) and by the ;235 compound' in the presence of an enzyme, the NADH(2)-oxidizing enzyme, present in extracts of lactoperoxidase-resistant streptococci. Sulphur dicyanide also acted as an electron acceptor in the latter reaction. The ;235 compound' was also reduced non-enzymically by sulphite. 3. The glycolysis of lactoperoxidasesensitive streptococci suspended in glucose solution was not inhibited by sulphite, cyanate, cyanide or the ;235 compound' but was inhibited by sulphur dicyanide. The inhibition by 0.1mm-sulphur dicyanide could be reversed, as could that caused by lactoperoxidase, thiocyanate and hydrogen peroxide, by washing the cells or by the addition of a cell-free extract of a lactoperoxidase-resistant streptococcus. 4. The effects of 0.1mm-sulphur dicyanide on catabolic enzymes of resting streptococci were very similar to those of the lactoperoxidase-thiocyanate-hydrogen peroxide system. Thus hexokinase was completedly inhibited, glucose 6-phosphate dehydrogenase and aldolase were partially inhibited and phosphohexokinase was little affected in both cases.
 ...
PMID:The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The oxidation of thiocyanate and the nature of the inhibitory compound. 533 6

Cell-free extracts of 17 strains of Bifidobacterium bifidum (Lactobacillus bifidus) were examined for the presence of aldolase, glucose-6-phosphate dehydrogenase, and fructose-6-phosphate phosphoketolase. All strains turned out to lack aldolase, an enzyme unique to glycolysis, and glucose-6-phosphate dehydrogenase, characteristic of the hexosemonophosphate pathway. In all strains, fructose-6-phosphate phosphoketolase could be demonstrated. It can be concluded that bifidobacteria ferment glucose via a pathway which is different from those found in members of the genus Lactobacillus. The results strengthen the previous suggestions that classification of the bifidobacteria in the genus Lactobacillus is not justified.
 ...
PMID:Pathway of glucose fermentation in relation to the taxonomy of bifidobacteria. 602 May 62

Histochemical studies have been conducted by applying hexokinase (HK), aldolase (AD), glyceraldehyde-3-phosphate dehydrogenase (G3), succinate dehydrogenase (SDH), glucose-6-phosphate dehydrogenase (G6PD), and thiamine pyrophosphatase (TPPase) methods, as well as Nissl staining and Gomori's chrome-alum-hematoxylin-phloxine (CHP) methods to intercalated neurons of the supraoptic nucleus (SO) on Wistar strain rats. Intercalated neurons reacted weakly to the AD, G3, G6PD, and SDH tests, indicating that they belong to the category of ordinary neurons with low carbohydrate metabolism. Many fibrous astrocytes showing strong HK reactions surround neurosecretory neurons. However, they do not surround intercalated neurons with mild HK activity. These results indicate that the latter receive a poor supply of energy from glucose in the circulating blood in contrast to the former. Intercalated neurons are very rich in Nissl substance but lack CHP-positive material. They may have a high potential for synthesizing protein. The principal morphological features of the TPPase-positive Golgi material are peculiar and heterogeneous shape and poor development. These findings together with mild G6PD activity suggest that intercalated neurons are very likely to have poor synthesizing activity.
 ...
PMID:Histochemical studies on the distribution of thiamine pyrophosphatase and enzymes related to carbohydrate metabolism in the intercalated neurons of the rat supraoptic nucleus. 613 41

Red cell enzymes, 2,3-diphosphoglycerate (2,3-DPG) and adenosine triphosphate (ATP), were evaluated in a 23-mo-old boy with juvenile chronic myelocytic leukemia (JCML) at the onset of his illness and 6 mo later during the accelerated phase. The activities of the age-dependent red cell enzymes, hexokinase, aldolase, pyruvate kinase, and glucose-6-phosphate dehydrogenase, were elevated, as were the concentrations of red cell 2,3-DPG and ATP, consistent with a young red cell population metabolizing at an increased glycolytic rate. The activities of the non-age-dependent enzymes, glyceraldehyde-3-phosphate dehydrogenase (G3PD), phosphoglycerate kinase, and enolase, were also increased to levels similar to or greater than those observed in term infants. As the illness progressed, the activity of red cell G3PD increased further, and phosphoglucose isomerase activity increased markedly. These results are consistent with the prior suggestion that JCML represents a reversion to "fetal" erythropoiesis.
 ...
PMID:Fetal erythropoiesis in juvenile chronic myelocytic leukemia. 622 20

The activities of key enzymes of glycolysis and of the glucose shunt as well as the capacity of lactic acid formation were determined in the high-speed tissue supernatant of the transplantable Albert hepatoma of mouse [originally produced by oral application of chrysoidin (2,4-diaminoazobenzene) on C57 Black mice]. Furthermore, the particle-bound hexokinase activity was determined. The following results were obtained: In the hepatoma the activities of aldolase, pyruvate kinase and lactic dehydrogenase are hardly altered compared with normal liver. The activities of hexokinase and phosphofructokinase are increased 2,5-fold, those of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase 2-fold. The capacity for lactic acid formation from glucose is 7 times as high in the hepatoma supernatant. Strong differences emerge from the liver-to-hepatoma relationship in terms of intracellular distribution of the hexokinase (total homogenate 1 : 5, supernatant 1 : 2,5 and particle-bound hexokinase activity 1 : 18). A summarizing consideration of all the results obtained so far for the Albert hepatoma shows that this malignoma departss in several biochemical parameters from the "Molecular Correlation Concept" maintained by Weber, providing more evidence for the individuality of tumors.
 ...
PMID:[Activities of several enzymes of glycolysis and of the glucose shunt in the Albert hepatoma of mouse (author's transl)]. 625 66


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>