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 primary structure of the muscle aldolase molecule was studied as affected by semilethal doses of valine administered the abdominal cavity of the rabbits after a long fasting. It is established that in spite of differences in the amino acid composition of the protein, uniformity of the peptides distribution in the process of bromo-cyanogen fragments elution and the total amount of amino acid residues in the identical fragments are maintained. Changes are found only in the point-replacements by amino acids in C-fragment of the molecule (asparagine is replaced by valine and threonine by serine).
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PMID:[Changes in the primary structure of rabbit muscle aldolase under the influence of valine against a background of prolonged fasting]. 102 17

Generation of antibodies and direct protein sequencing were used to identify and characterize proteins associated with highly purified synaptic vesicles from rat brain. A protein doublet of low abundance of 119 and 124 kDa apparent molecular mass [synaptic vesicle-associated phosphoprotein with a molecular mass of 120 kDa (SVAPP-120)] was identified using polyclonal antibodies. SVAPP-120 was found to copurify with synaptic vesicles and to be enriched in the purified synaptic vesicle fraction to the same extent as synapsin I. Like synapsin I, SVAPP-120 is not an integral membrane protein because it was released from synaptic vesicles by high salt concentrations. This protein was demonstrated to be brain specific, and its distribution in various brain regions paralleled the distribution of synapsin I and synaptophysin. During the postnatal development of the rat cortex and cerebellum, its expression correlated with synaptogenesis. SVAPP-120 was demonstrated to be a phosphoprotein both in vivo and in vitro. It was shown to be phosphorylated on serine and to a lesser extent on threonine residues. These results provide evidence that SVAPP-120 represents a novel synaptic vesicle-associated phosphoprotein. In addition, aldolase, a glycolytic enzyme, and alpha c-adaptin, a clathrin assembly-promoting protein, were identified on purified synaptic vesicles by direct protein sequencing.
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PMID:A novel synaptic vesicle-associated phosphoprotein: SVAPP-120. 207 93

The biosynthesis in vivo of a number of amino acids, sugars, and purines in Paracoccus denitrificans grown on either [2,3-13C]succinate or [1,4-13C]succinate was investigated by using gas chromatography-mass spectrometry. The distribution of label in the TCA-cycle-related amino acids indicated that carbon intermediates of energy metabolism were utilized as precursors for the biosynthesis of these amino acids in vivo. The biosynthesis of glycine, serine, phenylalanine and glycerol from labelled succinate in vivo were consistent with phosphoenol pyruvate as an intermediate. A mechanism for the formation of C4, C5 and C6 sugars without the use of fructose-1,6-bisphosphate aldolase (which has not been detected in P. denitrificans) is proposed. The 13C-enrichments of ribose in the bacterium indicate that there are at least three routes of ribose biosynthesis operating during growth on labelled succinate. The probability distribution of labelled purine molecules was successfully predicted for adenine, guanine and adenosine, thus confirming their generally accepted route of biosynthesis in vivo.
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PMID:Growth of Paracoccus denitrificans on [2,3-13C]succinate and [1,4-13C]succinate. III. Biosynthetic pathways. 289 30

The Mg,ATP-dependent serine proteinase (Mr = 50 kD; pH optimum 8.0) was isolated and purified 750-fold. The substrate specificity of the enzyme to some protein substrates (catalase, aldolase, uratoxidase, superoxide dismutase, albumin, cytochrome c, insulin) was investigated. The proteinase shows an affinity for proteins whose molecular mass is more than 100 kD. Some quantitative parameters of the enzyme metabolism, e.g., rate constants for synthesis and degradation of serine proteinase and the time of functioning of the de novo synthesized protein, were investigated.
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PMID:[Metabolism and various properties of proteinase controlling catalase metabolism in rat liver mitochondria]. 347 95

Changes in the content of dipicolinic acid and mineral elements were studied in the process of Bacillus thuringiensis spore germination. The spores released up to 28% of dipicolinic acid and 18% of calcium at the activation stage, and 93 and 91%, respectively, at the initiation stage. At the same time, the content of Mg, Mn, Zn and P decreased while K, Na and Fe accumulated in the spores. The activities of total and serine proteases, alkaline phosphatase, NADH dehydrogenase and aldolase increased in the extract of initiated spores. The content of glutamate decreased in the free amino acid pool as early as by the 30th second of the initiation stage.
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PMID:[Amino acid and mineral element content and the activity of various enzymes in germinating spores of Bacillus thuringiensis]. 389 44

The metabolism of hydroxyproline by the rat kidney leads to the production of significant quantities of both glycine and serine. This process was observed in both the isolated perfused kidney and in isolated cortical tubule suspensions. The rate of hydroxyproline metabolism was increased in both preparations by the addition of alanine. The distribution of hydroxyproline oxidase, hydroxyoxoglutarate aldolase and alanine-glyoxalate transaminase were determined in detail. All three enzymes were found exclusively in the renal cortex where they were restricted to the mitochondria. Cortical tubule fractionation studies indicated that the enzymes are located in the proximal convoluted and proximal straight segments at the nephron. The results suggest that hydroxyproline degradation could contribute significantly to the renal synthesis of serine.
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PMID:Hydroxyproline metabolism by the rat kidney: distribution of renal enzymes of hydroxyproline catabolism and renal conversion of hydroxyproline to glycine and serine. 393 Sep 16

d-arabino-3-Hexulose 6-phosphate was prepared by condensation of formaldehyde with ribulose 5-phosphate in the presence of 3-hexulose phosphate synthase from methane-grown Methylococcus capsulatus. The 3-hexulose phosphate was unstable in solutions of pH greater than 3, giving a mixture of products in which, after dephosphorylation, allulose and fructose were detected. A complete conversion of d-ribulose 5-phosphate and formaldehyde into d-fructose 6-phosphate was demonstrated in the presence of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase (prepared from methane-grown M. capsulatus). d-Allulose 6-phosphate was prepared from d-allose by way of d-allose 6-phosphate. No evidence was found for its metabolism by extracts of M. capsulatus, thus eliminating it as an intermediate in the carbon assimilation process of this organism. A survey was made of the enzymes involved in the regeneration of pentose phosphate during C(1) assimilation via a modified pentose phosphate cycle. On the basis of the presence of the necessary enzymes, two alternative routes for cleavage of fructose 6-phosphate are suggested, one route involves fructose diphosphate aldolase and the other 6-phospho-2-keto-3-deoxygluconate aldolase. A detailed formulation of the complete ribulose monophosphate cycle of formaldehyde fixation is presented. The energy requirements for carbon assimilation by this cycle are compared with those for the serine pathway and the ribulose diphosphate cycle of carbon dioxide fixation. A cyclic scheme for oxidation of formaldehyde via 6-phosphogluconate is suggested.
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PMID:The carbon assimilation pathways of Methylococcus capsulatus, Pseudomonas methanica and Methylosinus trichosporium (OB3B) during growth on methane. 437 54

Intraperitoneal administration of leupeptin to rats induced a hemoglobin-hydrolyzing protease which was most active at pH 3.5 and was insensitive to pepstatin in various tissues such as the liver, kidney, and muscle, as observed previously in adult rat hepatocytes in primary culture (Tanaka, K., Ikegaki, N., and Ichihara, A. (1979) Biochem. Biophys. Res. Commun. 91, 102-107). The induced acidic protease was purified about 600-fold in 30% yield from rat liver by conventional chromatographic techniques. The purified enzyme appeared homogeneous by polyacrylamide gel electrophoresis in the presence or absence of sodium dodecyl sulfate and was a monomeric protein of Mr = 20,000. The enzyme appeared to be a glycoprotein because its induction was blocked by the addition of tunicamycin to cultures of hepatocytes and because the induced protease was absorbed on concanavalin A-Sepharose and eluted with methylglucoside. It seemed to be present in lysosomes and was fairly stable at various pH values and temperatures. It showed endopeptidase activity on various protein substrates, but scarcely hydrolyzed N-substituted derivatives of arginine. It did not hydrolyze esters, showed no aminopeptidase or carboxypeptidase activity, and did not inactivate glucose-6-phosphate dehydrogenase or aldolase. The enzyme appeared to be a thiol protease, since it was strongly inhibited by sulfhydryl-reactive compounds and N-( [N-(1-3-trans-carboxyoxiran-2-carbonyl)-L-leucyl]-agmatine and was not inhibited by reagents specific for carboxyl-, serine-, or metalloproteases. This induced protease could be separated from cathepsins B, D, and H by chromatography. The enzyme was similar to cathepsin L in chromatographic behavior, Mr and pI, but differed from the latter in stability and in its inability to inactivate some enzymes. These results suggest that it differs from any known proteases found previously in rat liver.
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PMID:Purification and characterization of hemoglobin-hydrolyzing acidic thiol protease induced by leupeptin in rat liver. 637 Oct 12

Fructose-P2 aldolases isolated from vertebrate skeletal muscle have underivatized NH2-terminal proline residues in contrast to most other cytoplasmic proteins which contain alpha-N-acetylated termini. However, if "native" aldolase molecules derived from chicken muscle, rat liver, wheat germ, and the cytosol of spinach leaves are isolated in the presence of phenylmethanesulfonyl fluoride (an inhibitor of serine proteases), they contain blocked and presumably derivatized NH2-terminal residues. When chicken muscle aldolase is isolated in the absence of this protease inhibitor, the derivatized NH2-terminal residue is removed by an endogenous protease(s). The native and modified forms of the enzyme were not distinguished on the basis of catalytic activity, thermal stability, electrophoretic mobility, or subunit molecular weight. Structural analyses of both forms, together with amino acid sequence analysis of the primary translation product encoded for by aldolase mRNA, showed that native muscle aldolase subunits contain a single derivatized methionine NH2-terminal to the proline residue. This form of the enzyme is presumably the one which exists in vivo.
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PMID:Cellular fructose-P2 aldolase has a derivatized (blocked) NH2 terminus. 669 79

Anaerobically grown Staphylococcus epidermidis fermented glucose with the production of lactate and trace amounts of acetate, formate and CO2. Isotopic and inhibitor studies, assays for key enzymes of different metabolic pathways, and fermentation balances, all indicated that glucose was metabolized principally via glycolysis and to a very limited extent by the hexose monophosphate oxidative pathway. Serine fermentation proceeded via deamination and dismutation yielding NH3 and equimolar amounts of lactate, acetate and CO2; small amounts of formate arose by the operation of pyruvate-formate lyase. Incorporation of 0.5% (w/v) glucose in the growth medium depressed serine metabolism by repressing the activities of serine dehydratase and pyruvate dehydrogenase but, conversely, enhanced the activities of phosphofructokinase and lactate dehydrogenase. Glucose-grown organisms at various stages of anaerobic batch growth showed an inverse relationship between the rates of fermentation of serine and glucose. L-Lactate dehydrogenase activity in crude extracts depended on fructose 1,6-bisphosphate, and fructose 1,6-bisphosphate aldolase was found to be a class I aldolase. Despite the presence of ribokinase, D-ribose-5-phosphate isomerase, transaldolase and transketolase, the organisms utilized ribose only after growth aerobically in basal medium, and then at a slow rate after an initial lag period.
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PMID:Anaerobic glucose and serine metabolism in Staphylococcus epidermidis. 677 45


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