Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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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)

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

During the relatively recent period in which normal genes for most red cell enzymes have been isolated, the techniques of molecular biology have been applied to the studies of erythroenzymopathy. Single nucleotide substitutions have been identified in aldolase, triosephosphate isomerase, glucose 6-phosphate dehydrogenase, and adenylate kinase variants by the cloning and nucleotide sequence of the patients' genes. Up to now, all of the enzyme-deficient variants which have been investigated have been caused by point mutations. An exception is a hemolytic anemia secondary to increased adenosine deaminase (ADA) activity. Red cell ADA activity increases on the order of a hundred-fold in affected individuals. The basic abnormality appears to result from overproduction of structurally normal enzyme due to abnormal transcriptional or translational efficiency.
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PMID:Recent progress in the molecular genetic analysis of erythroenzymopathy. 216 22

In the past few years, very rapid advances have been made in the field of red cell enzymopathies associated with hereditary nonspherocytic hemolytic anemia, particularly in molecular basis. Nucleotide sequence and amino acid sequence of normal human red cell enzymes have been clarified in phosphofructokinase, aldolase, triosephosphate isomerase, phosphoglycerate kinase, pyruvate kinase, diphosphoglycerate mutase, glucose 6-phosphate dehydrogenase, adenylate kinase and adenosine deaminase. Furthermore, in aldolase-, triosephosphate isomerase-, diphosphoglycerate mutase-, glucose 6-phosphate dehydrogenase-, and adenylate kinase deficiency, single nucleotide changes which cause single amino acid substitutions and finally hemolysis, have been found.
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PMID:Molecular basis of red cell enzymopathies associated with hereditary nonspherocytic hemolytic anemia. 256 Apr 52

Since the discovery of glucose-6-phosphate dehydrogenase (G6PD) deficiency and pyruvate kinase deficiency, erythroenzymopathies associated with hereditary hemolytic anemia have been extensively investigated. Kinetic and electrophoretic studies have shown that most erythroenzymopathies are caused by the production of a mutant enzyme. Single amino acid substitutions have been determined in G6PD and phosphoglycerate kinase variants by studies of the enzyme. Except for these two enzymes, it has been difficult to purify and to characterize the patient's enzyme because of the low protein contents in red blood cells. Recent advance in recombinant DNA technology has made possible the isolation of normal genomic DNA or cDNA for several enzymes. These results permit us to study the molecular basis of erythroenzymopathies at the nucleotide level. Single base substitutions have been identified in aldolase, triosephosphate isomerase, G6PD and adenylate kinase variants by the cloning and nucleotide sequence of the patients' genes. To date, all of the enzyme-deficient variants which have been investigated are caused by point mutations. An exception is a hemolytic anemia secondary to increased adenosine deaminase (ADA) activity. Red cell ADA activity increases on the order of a hundred-fold in affected individuals. The basic abnormality appears to result from overproduction of structurally normal enzyme due to abnormal translational efficiency.
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PMID:[Pathophysiology and laboratory tests of hemolytic anemia: with special reference to erythroenzymopathies]. 269 73

Since the discovery of glucose 6-phosphate dehydrogenase (G6PD) and of pyruvate kinase deficiencies, erythroenzymopathies associated with hereditary hemolytic anemia have been extensively investigated. Kinetic and electrophoretic studies have shown that most, if not all, erythroenzymopathies are caused by the production of a mutant enzyme. Except for a few enzymes that are abundant in blood and tissues, it is difficult to obtain enough sample to study the functional and structural abnormalities of mutant enzymes associated with genetic disorders in man. The primary structures of only two normal red cell enzymes which can cause hereditary hemolytic anemia, phosphoglycerate kinase (PGK) and adenylate kinase, have been determined. Single amino acid substitutions of PGK variants have been found, and the identification of the exact molecular abnormalities of such variants has helped us to understand the accompanying functional abnormality. Gene cloning makes possible the identification of the DNA sequence that codes for enzyme proteins. Recently, human complementary DNA (cDNA) for aldolase, PGK, G6PD, and adenosine deaminase (ADA) have been isolated, and the nucleotide sequences for PGK and ADA determined. In the near future, human cDNA sequencing should permit identification of the gene alteration that gives rise to the mutant enzymes.
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PMID:Molecular aspects of erythroenzymopathies associated with hereditary hemolytic anemia. 299 Feb 2

Enzymes of the glycolytic pathway as well as some ancillary enzymes were studied in normal red cells parasitized with Plasmodium falciparum in culture at varying parasitemias as well as in isolated parasites. The levels of all enzymes except diphosphoglycerate mutase, glucose-6-phosphate dehydrogenase, and adenylate kinase were elevated. Extreme elevations of hexokinase, aldolase, enolase, pyruvate kinase, and adenosine deaminase concentrations were noted. In most cases, electrophoretically distinct bands of enzyme activity were also seen. These findings partly explain the previously noted 50- to 100-fold increase in glucose consumption of infected red cells and suggest that further knowledge of these parasite enzymes and their genetic basis may aid both in designing new chemotherapy and in understanding the evolution of these parasites.
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PMID:The enzymes of the glycolytic pathway in erythrocytes infected with Plasmodium falciparum malaria parasites. 305 30

In Bacillus cereus purine ribonucleosides and deoxyribonucleosides share a common inducible catabolic pathway, leading to the formation of ribose-5-P or deoxyribose-5-P respectively inside the cell, while the purine ring remains in the external medium. Both ribo- and deoxyribonucleosides are inducers of adenosine deaminase, inosine-guanosine phosphorylase and phosphopentomutase, the enzymes of the catabolic pathway. We now show that deoxyribonucleosides, but not ribonucleosides, induce the aldolase specific for deoxyribose-5-P (2-deoxy-D-ribose-5-phosphate acetaldehyde lyase, EC 4.1.2.4), thus allowing the sugar moiety of exogenous deoxyribonucleosides to be utilized as an energy source.
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PMID:Induction of deoxyribose-5-phosphate aldolase of Bacillus cereus by deoxyribonucleosides. 643 5

Studies on the adenosine deaminase (ADA) and aldolase activities in lymphocytes were performed in 67 patients with glomerulonephritis (gn) and in 20 healthy individuals from the control group to get an insight into the lymphocyte metabolism. Statistically significant decrease of ADA activity was found in the groups of patients with chronic proliferative gn, membranoproliferative gn, membranous gn and lupus nephritis in comparison with the healthy individuals from the control group. As far as decrease of aldolase activity is concerned it has reached statistical significance in patients with mesangial gn, membranoproliferative gn, membranous gn and lupus nephritis. The lymphocyte metabolism did not show any abnormalities in the enzymatic indicators only in patients with acute proliferative gn and submicroscopic gn. The activity comparison between both enzymes in the lymphocytes, contrasted on the basis of high and low clinical dynamics of gn, revealed a tendency to lower ADA and aldolase activities in patients with high clinical dynamics. However, this difference was at the limit of statistical significance (p less than or equal to 0.10).
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PMID:Aldolase and adenosine deaminase activity in lymphocytes of patients with glomerulonephritis. 665 34

The molecular abnormalities of erythroenzymopathies associated with hereditary hemolytic anemia have been determined using molecular techniques. Pyruvate kinase (PK) deficiency is the most common and well-characterized enzyme deficiency involving the glycolytic pathway and causing hereditary hemolytic anemia. We have identified six distinct missense mutations and a form of splicing mutation in 11 unrelated families with homozygous PK deficiency. Mutations located near the substrate binding site may change the conformation of the active site, resulting in a drastic loss of activity and severe clinical symptoms. Up to now, including these genetic defects, 21 missense, 1 nonsense and 2 splicing mutations, 2 insertions, and 3 deletions have been determined. G6PD deficiency is the most common metabolic disorder, and is associated with chronic and drug- or infection-induced hemolytic anemia. To date, sixty different mutations have now been identified. Except for three kinds of variants with small gene deletions or three nucleotide substitutions, all of those were found to be produced by one or two nucleotide substitutions. Molecular studies disclosed that all the class 1 variants associated with chronic hemolysis have the mutations surrounding either the substrate or the NADP binding site. Among rare enzymopathies, missense mutations have been determined in glucosephosphate isomerase deficiency, aldolase deficiency, triosephosphate isomerase (TPI) deficiency, phosphoglycerate kinase deficiency, and adenylate kinase deficiency. Compound heterozygous cases with missense mutation/nonsense mutation and missense mutation/decreased mRNA have been reported in TPI deficiency and diphosphoglyceromutase deficiency, respectively. In phosphofructokinase (PFK) deficiency, three kinds of 5'-splice junction mutations resulting in abnormally spliced PFK-M mRNA were identified. An exception is a hemolytic anemia due to increased adenosine deaminase activity. The basic abnormality appears to result from overproduction of structurally normal enzyme.
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PMID:Red cell enzymopathies as a model of inborn errors of metabolism. 862 88

We examined the possible implication of ras in the regulation of the activity of several metabolic enzymes by employing an inducible H-ras expression system (RFLSVrasLAP cell line), in which the addition of IPTG decreases the levels of ras p21 3-fold. We measured the activity of hexokinase (E.C. 2.7.1.1.), glucose phosphate isomerase (E.C. 5.3.1.9), phospho-fructokinase (E.C. 2.7.1.11), aldolase (E.C. 4.1.2.13), phosphoglycerate kinase (E.C. 2.7.2.3), enolase (E.C. 4.2.1.11), pyruvate kinase (E.C. 2.7.1.40), lactate dehydrogenase (E.C. 1.1.1.27), adenosine deaminase (E.C. 3.5.4.4) and purine nucleoside phosphorylase (E.C. 2.4.2.1) from cells grown in the presence and absence of IPTG. We found that the addition of IPTG to RFLSVrasLAP cells led to lower activity of phosphoglycerate kinase (p=0.004), enolase (p=0.027) and pyruvate kinase (p=0.031). Enolase mRNA levels were found to be increased in cells overexpressing either the normal or mutant H-ras. The total rate of glycolysis was not affected by H-ras expression indicating that the implication of H-ras in the activity of phosphoglycerate kinase, enolase and pyruvate kinase may be associated with glycolysis-independent functions of these enzymes. Adenosine deaminase activity was found to increase after IPTG addition (P=0.009), indicating also a possible role for H-ras in the control of the purine nucleotide salvage pathway.
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PMID:T24 h-ras gene-expression increases the activity of phosphoglycerate kinase, enolase and pyruvate-kinase and decreases the activity of adenosine-deaminase in fibroblast cells. 2160 14


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