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)

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.
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PMID:Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue during germination. 438 39

Wild-type Escherichia coli cannot grow on L-1,2-propanediol; mutants that can do so have increased basal activity of an NAD-linked L-1,2-propanediol oxidoreductase. This enzyme belongs to the L-fucose system and functions normally as L-lactaldehyde reductase during fermentation of the methylpentose. In wild-type cells, the activity of this enzyme is fully induced only anaerobically. Continued aerobic selection for mutants with an improved growth rate on L-1,2-propanediol inevitably leads to full constitutive expression of the oxidoreductase activity. When this occurs, L-fuculose 1-phosphate aldolase concomitantly becomes constitutive, whereas L-fucose permease, L-fucose isomerase, and L-fuculose kinase become noninducible. It is shown in this study that the noninducibility of the three proteins can be changed by two different kinds of suppressor mutations: one mapping external to and the other within the fuc gene cluster. Both mutations result in constitutive synthesis of the permease, the isomerase, and the kinase, without affecting synthesis of the oxidoreductase and the aldolase. Since expression of the fuc structural genes is activated by a protein specified by the regulator gene fucR, and since all the known genes of the fuc system are clustered at minute 60.2 of the chromosome, the external gene in which the suppressor mutation can occur probably has an unrelated function in the wild-type strain. The internal suppressor mutation might be either in fucR or in the promoter region of the genes encoding the permease, the isomerase, and the kinase, if these genes belong to the same operon.
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PMID:Constitutive activation of L-fucose genes by an unlinked mutation in Escherichia coli. 637 90

The alpha-ketoglutarate dehydrogenase complex of either pig heart or Escherichia coli catalyzes a NAD- and CoASH-dependent oxidation of 2-keto-4-hydroxyglutarate which is stereoselective toward the L-isomer of this hydroxyketo acid. L-Malyl-CoA is the product of the reaction; the evidence includes observing (a) a steady increase in absorbance at 230 nm during the oxidation of 2-keto-4-hydroxyglutarate, (b) a positive response of oxidation reaction mixtures to neutral hydroxylamine, (c) loss of the two foregoing results concomitant with release of thiol-reacting material and the formation of free malate when reaction mixtures are heated, (d) formation of a hydroxamate which has chromatographic mobilities identical to that of chemically synthesized malate hydroxamate, (e) enzymatic formation of a radioactive product from 14C-labeled 2-keto-4-hydroxyglutarate which co-migrates with chemically synthesized malyl-CoA, and (f) hydrolysis of the product by citrate synthase, an enzyme absolutely specific for citryl-CoA and L-malyl-CoA. A 1:1:1 stoichiometric relationship exists between the amount of 2-keto-4-hydroxyglutarate oxidized, NAD reduced, and malate (or malyl-CoA) formed. Results from studies in which either 14C-labeled 2-keto-4-hydroxyglutarate, pyruvate, or glyoxylate is incubated with mixtures of purified enzymes or extracts of E. coli support the suggestion that the aldolase which preferentially catalyzes formation of L-2-keto-4-hydroxyglutarate from pyruvate plus glyoxylate in E. coli is coupled with the oxidative decarboxylation of this substrate, as reported here, and other enzymes in a multistep pyruvate-catalyzed cyclic oxidation of glyoxylate.
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PMID:Malyl-CoA formation in the NAD-, CoASH-, and alpha-ketoglutarate dehydrogenase-dependent oxidation of 2-keto-4-hydroxyglutarate. Possible coupled role of this reaction with 2-keto-4-hydroxyglutarate aldolase activity in a pyruvate-catalyzed cyclic oxidation of glyoxylate. 638 79

A simple, highly specific, and sensitive bioluminescent method for determination of free fatty acids in unextracted plasma or serum has been developed. The method is based on the activation of free fatty acids by acyl-CoA synthetase (EC 6.2.1.3). The pyrophosphate formed is used to phosphorylate fructose 6-phosphate in a reaction catalyzed by the enzyme pyrophosphate-fructose-6-phosphate phosphotransferase (EC 4.1.2.13). The triosephosphates produced from fructose 1,6-bisphosphate by aldolase are oxidized by NAD in the presence of arsenate to 3-phosphoglycerate. The NADH is detected via the bacterial NADH-linked luciferase system. Excellent agreement has been obtained by comparison with accepted methods. In addition, for the determination of serum free fatty acids, the method is particularly applicable for following lipolysis of isolated adipocytes.
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PMID:Bioluminescent determination of free fatty acids. 648 22

Isozyme patterns of 23 different enzymes were compared in normal, benign, and malignant breast tissues; in MCF-7 cells; and in organoids of normal human breast tissue. Benign lesions generally showed isozyme patterns similar to those of normal tissues. Lactate dehydrogenase isozyme 5 was significantly increased in malignant tumors; MCF-7 cells had only lactate dehydrogenase (L-lactate:NAD oxidoreductase; EC 1.1.1.27). The mitochondrial form of malate dehydrogenase was also significantly increased in human malignant tumors; this was especially evident when comparing tumor and apparently uninvolved breast tissue from the same patient. The K4 isozyme of pyruvate kinase was the major form in most malignant breast tumors, but in only 41% of normal tissues, 30% of fibrocystic disease specimens, and 46% of fibroadenomas. A more anodal band of pyruvate kinase, probably a K3M or K3Kpm hybrid, predominated in most normal and benign tissues, but in only 63% of primary and 56% of secondary tumors. All specimens had predominantly creatine kinase BB, aldolase A4, and hexokinase I. Traces of aldolase A3C and of hexokinase II were observed in some tumors. None of the tumors had the Regan variant of alkaline phosphatase. The isozymes of lactate and malate dehydrogenases and of pyruvate kinase appear to be the most promising as putative tumor markers.
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PMID:Isozyme patterns of normal, benign, and malignant human breast tissues. 664 May 38

1. With fumarate as the terminal electron acceptor and either H2 or formate as donor, Vibrio succinogenes could grow anaerobically in a mineral medium using fumarate as the sole carbon source. Both the growth rate and the cell yield were increased when glutamate was also present in the medium. 2. Glutamate was incorporated only into the amino acids of the glutamate family (glutamate, glutamine, proline and arginine) of the protein. The residual cell constituents were synthesized from fumarate. 3. Pyruvate and phosphoenolpyruvate, as the central intermediates of most of the cell constituents, were formed through the action of malic enzyme and phosphoenolpyruvate synthetase. Fructose-1,6-bisphosphate aldolase was present in the bacterium suggesting that this enzyme is involved in carbohydrate synthesis. 4. In the absence of added glutamate the amino acids of the glutamate family were synthesized from fumarate via citrate. The enzymes involved in glutamate synthesis were present. 5. During growth in the presence of glutamate, net reducing equivalents were needed for cell synthesis. Glutamate and not H2 or formate was used as the source of these reducing equivalents. For this purpose part of the glutamate was oxidized to yield succinate and CO2. 6. The alpha-ketoglutarate dehydrogenase involved in this reaction was found to use ferredoxin as the electron acceptor. The ferredoxin of the bacterium was reoxidized by means of a NADP-ferredoxin oxidoreductase. Enzymes catalyzing the reduction of NAD, NADP or ferredoxin by H2 or formate were not detected in the bacterium.
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PMID:Biosynthetic Pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source. 710 60

NAD-Sepharose 4B gel was used to study the complexation between glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating) EC 1.2.1.12) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13). An affinity sorbent specific for glyceraldehyde-3-phosphate dehydrogenase was utilised in a batch system. The dissociation constant of the enzyme complex was calculated. The method elaborated in our laboratory was used to investigate the effects of temperature and pH on the complex formation.
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PMID:Characterization of enzyme-enzyme interaction using an affinity batch system. 710 69

A direct interaction of rabbit muscle fructose-1,6-bisphosphate aldolase with NAD+, NADH, and NAD-agarose was demonstrated. The electrostatic forces are primary involved in this interaction. Two specific binding sites for the dinucleotide were observed. One of them is located at the active site of the enzyme, the second is in a region of weak binding site for ATP and fructose 1,6-bisphosphate.
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PMID:Binding of nicotinamide-adenine dinucleotide to rabbit muscle aldolase. 737 Feb 81

The halophilic archaea display a considerable extent of enzyme diversity. The presence or absence of certain enzymatic activities is closely linked with the taxonomic status of the strains investigated. Thus, Halobacterium species such as Hb. salinarium, Hb. halobium, and Hb. cutirubrum differ from most other Halobacteriaceae tested by the possession of an NAD(+)-dependent glycerol dehydrogenase, by the absence of methylglyoxal synthase activity, and the ability of fermentative growth on arginine. Species such as Hb. saccharovorum and Hb. sodomense, which are still classified within the genus Halobacterium, have an enzymatic machinery greatly different from that of the Hb. salinarium-Hb. halobium group, confirming the need for a taxonomic reappraisal of these species. The presence of NAD(+)-dependent D-lactate dehydrogenase is characteristic of representatives of the genus Haloarcula, which possess only low activities of NAD(+)-independent L- and D-lactate dehydrogenases, if at all. Other enzymes which show considerable diversity are fructose 1,6-bisphosphate aldolase, of which two classes exist, and ribulose 1,6-bisphosphate carboxylase, which is present in a limited number of species.
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PMID:Enzyme diversity in halophilic archaea. 787 98

The objective of this study was to determine whether the concentration of pyridine nucleotides in muscle and liver tissue of quail affected the heat stability of aldolase and selected enzymes involved in the oxidation-reduction of these cofactors. The thermal stability of malic enzyme, glyceraldehyde-3-phosphate dehydrogenase, lactic dehydrogenase, and aldolase in liver, and in pectoral muscle of quail was studied at incubation temperatures ranging from 27 to 60 degrees C. The concentrations of liver NAD, NADP, NADPH and the thermal inactivation of liver malic enzyme, glyceraldehyde-3-phosphate dehydrogenase, lactic dehydrogenase, and aldolase were not affected by niacin deficiency. In contrast, pectoral muscle glyceraldehyde-3-phosphate dehydrogenase in the niacin deficient quail compared to that of the controls had a markedly reduced thermal stability. This was associated with a corresponding decrease in the concentration of NAD and possibly NADPH. However, lactic dehydrogenase and aldolase activities were not affected. A similar pattern of heat inactivation was obtained when dialysed muscle and liver extracts were spiked with NAD or NADP. In these studies, NAD(P) protected muscle glyceraldehyde-3-phosphate dehydrogenase against heat inactivation to a much greater degree than that obtained with the other enzymes from muscle or liver tissue. These results suggest a causative relationship between the thermal stability of glyceraldehyde-3-phosphate dehydrogenase and coenzyme status in pectoral muscle tissue. This effect of niacin deficiency on the thermal stability of enzymes appears to be quite selective and specific.
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PMID:Effect of niacin deficiency on the thermal stability of NAD- and NADP-dependent dehydrogenases in liver and pectoral muscle of Japanese quail. 893 Jan 42


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