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)

Blood serum was used of 49 rams and 20 ewew infected with Brucell ovis. The study on the total protein and the protein fractions of rams revealed that there existed gamma-globulinemia, the percent of the gamma-globulin rise showing a positive correlation with the morphologic changes in the testes. The alfa-globulins were found to rise immediately following the experimental infecting of the sheep for about a month, after which they came back to normal. In experimental infection the activity of the alkaline phosphatase, aldolase, glutamate-oxalacetate-transaminase, and glutamate-pyruvate-transaminase of the blood serum showed transient characteristic changes, having, however, no diagnostic value.
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PMID:[Biochemical study of serum from sheep infected with Brucella ovis]. 8 49

Enzyme activity of lactate dehydrogenase, glutamate-oxalacetate and glutamate-pyruvate transaminase, creatine phosphokinase, cholinesterase, alkaline, acid and prostatic phosphatase and aldolase has been studied in a total of 213 subjects, of whom 97 were of good health, 63 had bone tumors and 53 suffered from osteomyelitis. The activities of the majority of the enzymes were found to become significantly changed in comparison with the norm. In both patient groups, the more striking differences being noted in that of osteomyelitis. However, enzymatic activity alone does not allow to differentiate the group of bone tumors from that of osteomyelitis, the differences between these two groups not being of significance in any one of the enzymes followed.
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PMID:Serum enzyme activity in bone tumors and osteomyelitis (LDH, GOT, GPT, CPK, CHE, ALP, AP, PP, ALD). 19 May 48

The activity of the following enzymes in clinically normal newborn calves was investigated: glutamate-oxalacetate transaminase (GOT), glutamate-pyruvate transaminase (GPT), alkaline phosphatase (APh), creatine phosphokinase (CPhK), lactate dehydrogenase (LDH), leucine-aminopeptidase (LAP), aldolase (A), and cholinesterase (ChE). The studies were carried out at the first hour prior to offering colostrum as well as at the 6th, 12th, 24th hr and on the 2nd, 3rd, 4th, 5th, 7th, 10th, 15th, and 20th day following it first intake. Regularly rising values of the enzyme activity up to the 24th hour were observed with APh, GOT, GPT, CPhK, and LAP. The aldolase enzyme (after colostrum had been given for the first time) in all animals showed a statistically significant drop of activity at the 6th hour. The activity of LDH displayed a consistently rising trend up to the end of the experimental period. The cholinesterase activity showed high values immediately following birth, reaching those found in the dams by the end of the observation period.
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PMID:[Dynamics of some serum enzymes in the postnatal development of calves]. 94 95

2-Keto-4-hydroxyglutarate aldolase, which catalyzes the reversible cleavage of 2-keto-4-hydroxyglutarate, yielding pyruvate plus glyoxylate, has been purified from extracts of bovine kidney to apparent homogeneity as judged by polyacrylamide gel electrophoresis, gel filtration chromatography, sucrose density gradient centrifugation, and meniscus depletion sedimentation equilibrium experiments. The enzyme from this source has a native and a subunit mass of 144 and 36 kDa, respectively; the pH-activity optimum is 8.8. Rather than being stimulated, aldolase activity is inhibited to varying degrees by added divalent metal ions, whereas a number of metal ion-chelating agents have no effect. An absolute requirement for added thiol compounds could not be shown, but 2-mercaptoethanol enhances activity 2-fold, and added Hg2+ as well as p-mercuribenzoate or dithiodipyridine markedly inhibit catalysis. Incubation of the enzyme with either pyruvate or glyoxylate in the presence of NaBH4 causes extensive loss of aldolase activity concomitant with stable binding of approximately 1.0-1.5 mol of 14C-labeled substrate/mol of enzyme. The circular dichroism spectrum for native aldolase is characteristic of an alpha-helix; incubation of the enzyme with glyoxylate has no effect on this spectrum, but it is considerably altered by pyruvate. Bovine kidney aldolase shows no stereospecificity in catalyzing the aldol cleavage of the two optical isomers of 2-keto-4-hydroxyglutarate, and although it also catalyzes the beta-decarboxylation of oxalacetate, its decarboxylase/aldolase activity ratio is lower than that seen with the pure enzyme from either bovine liver or Escherichia coli.
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PMID:2-Keto-4-hydroxyglutarate aldolase: purification and characterization of the homogeneous enzyme from bovine kidney. 158 31

Pure 2-keto-4-hydroxyglutarate aldolase of Escherichia coli, a "lysine-type" trimeric enzyme which has the unique properties of forming an "abortive" Schiff-base intermediate with glyoxylate (the aldehydic product/substrate) and of showing strong beta-decarboxylase activity toward oxalacetate, binds any one of its substrates (2-keto-4-hydroxyglutarate, pyruvate, or glyoxylate) in a competitive manner. To determine whether the substrates bind at the same or different (juxta-positioned) sites and what degree of homology might exist between the active-site lysine peptide of this enzyme and that of other lysine-type (Class I) aldolases or beta-decarboxylases, the azomethine formed separately by this aldolase with either [14C]pyruvate or [14C]glyoxylate was reduced with CNBH3-. After each enzyme adduct was digested with trypsin, the 14C-labeled peptide was isolated, purified, and subjected to amino acid analysis and sequence determination. In each case, the same 14-amino acid lysine-peptide was isolated and found to have the following primary sequence: Glu-Phe-*Lys-Phe-Phe-Pro-Ala-Glu-Ala-Asn-Gly-Gly-Val-Lys (where * = the active-site lysine). Hence, glyoxylate competes for, and inhibits aldolase activity by reacting with, the one active-site lysine residue/subunit. This active-site lysine peptide has a high degree (65%) of homology with that of 2-keto-3-deoxy-6-phosphogluconate aldolase of Pseudomonas putida but is not similar to that of any Class I fructose-1,6-bisphosphate aldolase or of acetoacetate beta-decarboxylase of Clostridium acetobutylicum. Furthermore, it was found that extensive reaction of glyoxylate with the N-terminal amino group of this enzyme may well be general complicating factor in sequence studies with proteins plus glyoxylate.
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PMID:Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. 309 43

Formation of a bienzyme complex of pig heart mitochondrial malate dehydrogenase and citrate synthase in a buffered system is demonstrated by means of a covalently attached fluorescent probe to citrate synthase. Assuming 1:1 stoichiometry of the enzymes in the complex, an apparent dissociation constant of 10(-6) M was calculated from fluorescence anisotropy measurements. The effect of various metabolites on the interaction was tested. NAD+, oxalacetate, citrate, ATP, and L(-)- or D(+)-malate had no effect on the association of the two enzymes, whereas alpha-ketoglutarate increased and NADH decreased it. The interaction of mitochondrial citrate synthase with cytosolic malate dehydrogenase was found to be much weaker, whereas interaction of citrate synthase with another cytosolic enzyme, aldolase, could not be detected. In kinetic experiments, the activation of malate dehydrogenase by citrate synthase was observed. The effect of pyridine nucleotides and alpha-ketoglutarate is discussed in relation to the direction of the metabolic flow of oxalacetate.
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PMID:Quantitation of the interaction between citrate synthase and malate dehydrogenase. 357 Dec 48

The enzyme 4-hydroxy-2-ketoglutarate aldolase (4HKG aldolase), which catalyzes the reversible cleavage of 4-hydroxy-2-ketoglutarate to form pyruvate and glyoxylate, was isolated from rat liver. The purification scheme as well as a study of several of the physical and kinetic properties of the enzyme are presented. The effects of anions, various buffers, and possible physiologically relevant effectors on the kinetic parameters of the aldolase were also investigated. It was found that pyruvate analogs inhibited the aldolase. Oxaloacetate was a competitive inhibitor of the aldolase, and in addition caused synergistic inhibition with respect to pyruvate analogs at low substrate concentration. These results are discussed in terms of possible regulation of the aldolase.
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PMID:Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization. 396 4

Infection of white rats with Francisella tularensis (Pasteurella tularensis) and Salmonella typhimurium and exposure to the endotoxin of S. typhimurium stimulated significant increases in various serum enzymes including aldolase, lactate dehydrogenase, phosphohexose isomerase, isocitrate dehydrogenase, and glutamate-oxalacetate transaminase. The rates of changes in enzymatic activity after infection were directly related to the size of infecting dose and to the type of infective agent employed. Tularemic infection stimulated excessive changes in enzyme activity, whereas salmonellosis and endointoxication elicited less pronounced alterations of relatively short duration. Changes observed in serum enzymes after exposure to these agents reflect the severe liver damage and extensive systemic involvement noted in tularemia as opposed to more localized and less intensive tissue damage occurring during salmonellosis and endointoxication.
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PMID:Influence of bacterial infection on serum enzymes of white rats. 488 56

Microfilariae of bovine filarial parasite Setaria cervi are equipped with the enzymes of glycolysis, pentose phosphate and PEP-succinate pathways and thus resemble the adult form in its metabolic pattern. Malate dehydrogenase was the most active enzyme in microfilariae followed by lactic dehydrogenase and fumarase, while phosphoglucoisomerase, PEP-carboxykinase and FDP-aldolase were comparatively less active. The very low ratio of PK/PEPCK in S. cervi microfilariae indicates active fixation of CO2 into PEP to produce oxalacetate. Centperazine and diethylcarbamazine significantly inhibited PEP-carboxykinase, fumarate reductase and succinic dehydrogenase, suggesting that these antifilarials probably exert microfilaricidal action by blocking the PEP-succinate pathway.
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PMID:Setaria cervi: enzymes in microfilariae and in vitro action of antifilarials. 715 43

Studied was the dynamics of the changes taking place in the activity of a number of enzymes in the blood plasma (glutamate oxalacetate transaminase (GOT), glutamate pyruvate transaminase (GPT), lactate dehydrogenase (LDH), alkaline phosphatase (AP), aldolase (ALD), creatine phosphokinase (CPK), guanase, and cholinesterase (CE). The calculation of the correlation coefficients and the regression lines revealed that GOT, GPT, LDH, ALD, and guanase raised their activity following treatment of the test animals up to a higher extent and at a higher rate. Lower rate changes were those in the activity of AP, leucinaminopeptidase, and CE. No changes whatever were found in the activity of CPK. On the basis of these results the diagnostic value is determined of both the individual enzymes and the enzyme constellation as a whole.
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PMID:[Changes in serum enzyme activity after the tetrachloromethane treatment of guinea pigs]. 716 46


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