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

---

Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenosine deaminase (ADA), 5'nucleotidase (5'NT), ecto-5'NT, purine nucleoside phosphorylase (PNP), hypoxanthine-guanine phosphoribosyltransferase (HGPRT), adenine phosphoribosyltransferase (APRT), adenosine kinase (AK), AMP-deaminase (AMPD) and adenylate kinase (AdKin) activities were assayed in peripheral blood lymphoid cells from 20 patients with B-cell type chronic lymphocytic leukemia (CLL). Significantly decreased mean activities of ADA, 5'NT, ecto-5'NT, PNP and AMPD were observed when comparing B-CLL lymphoid cells with control peripheral blood lymphocytes (PBL). AK and AdKin activities however, were found to be higher in B-CLL. Relatively wide ranges of ADA and 5'NT activity were observed. In patients with paraproteinaemia, 5'NT activity was found to be relatively high and in the range of the activities in normal PBL. ADA activity seemed to be slightly higher in patients without paraproteinaemia. No correlation could be found between the enzyme activities and the number of cells rosetting with sheep erythrocytes or bearing surface immunoglobulin (sIg). A relationship was suggested between 5'NT activity and Ig production.
...
PMID:Enzymological studies in chronic lymphocytic leukemia. 640 72

The use of high-performance liquid chromatography to identify and quantitate five purine-metabolizing enzymes from a partially purified subcellular fraction of the eucaryotic microorganism Dictyostelium discoideum is described. All HPLC separations were carried out in an isocratic manner using reverse-phase C18 as the stationary phase. The mobile phase consisted of a phosphate buffer with either methanol or acetonitrile as cosolvent, and optimal separation conditions were attained by varying the organic concentration or the pH of the buffer or by employing paired-ion chromatographic techniques. Substrates and products were detected at either 254 nm for the purines or 295 nm for the formycin analogs. An adenosine kinase activity was identified, and it was demonstrated that formycin A (FoA) could be substituted for adenosine as the phosphate acceptor, yielding FoAMP as the product. With FoA as the substrate an apparent Km of 18.2 microM and an apparent Vmax of 32.4 mmol min-1 mg-1 were observed for the activity. A purine-nucleoside phosphorylase activity was found to cleave adenosine to adenine and ribosylphosphate. FoA was not found to be a substrate for this activity due to the unusual formycin C-glycosyl bond which was not hydrolyzed by enzymes or chemically with either HCl or NaOH. An adenylate deaminase activity was found to be present in the cytosolic S-100 of cells harvested during the onset of development, and this deaminase activity was greatly stimulated by ATP. With FoAMP as the substrate, an apparent Km of 236 microM and Vmax of 2.78 mumol min-1 mg-1 were observed. The deamination of FoAMP could be inhibited by the addition of the natural substrate AMP. An apparent Ki value of 136 microM was determined from initial rate data. An adenylosuccinate synthetase activity was observed to have a Km value for GTP, IMP, and aspartic acid of 23, 34, and 714 microM, respectively. The formycin analog FoIMP was not a substrate with this activity but was a competitive inhibitor of IMP. Finally hypoxanthine-guanine phosphoribosyltransferase was found to have Km and Vmax values for hypoxanthine of 55.5 microM and 34.3 nmol-1 min-1 mg-1. When guanine was used as the substrate, the rate of nucleotide formation was 50% that with hypoxanthine as the substrate. The advantages of using HPLC to examine the interconnecting activities of a multienzyme complex in subcellular fractions are discussed, including the increased sensitivity obtained by using formycin analogs in the assay procedures.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Intermediary purine-metabolizing enzymes from the cytosol of Dictyostelium discoideum monitored by high-performance liquid chromatography. 642 68

Normal (line 200) and dystrophic (line 307) embryonic chicken pectoralis muscle cells were studied in cell culture over a period of 2 weeks. During the first 4 days, normal and dystrophic cultures exhibited similar developmental increases in the number of nuclei within multinucleated myotubes, however, dystrophic muscle cells degenerated approximately twice as fast as normal cells once the initial burst of myoblast fusion was complete. The apparent synthesis rate of nonmyofibrillar proteins was similar in normal aand dystrophic cells throughout development, but the apparent synthesis rates of myosin heavy chain and the myofibrillar protein fraction were 50%--90% higher in dystrophic muscle cultures once maturity had been reached (days 6--14). The specific activities of creatine kinase and phosphofructokinase were not affected by the dystrophic condition; however, specific activity of AMP-deaminase was depressed 25%--40% in the dystrophic muscle cultures.
...
PMID:Normal and dystrophic embryonic chicken pectoralis muscle cultures: I. Cell differentiation, protein synthesis, and enzyme levels. 645 4

Concentrations of key metabolites were determined in goldfish red muscle, while muscle and blood before and after direct electrical stimulation of the myotome (60 pulses/min, amplitude 500 mV, 10 msec pulse duration, during 10 min at 20 degrees C). In white muscle, levels of ATP, aspartate and adenylate energy charge are significantly lowered while those of AMP, IMP, NH3, alpha-ketoglutarate, lactate and malate are increased. In red muscle, the only change induced by stimulation is a 160% increase of the lactate level. In white muscle, IMP-accumulation and ammonia production are equal, suggesting the AMP-deaminase reaction to be the major source of muscular ammonia. Activation of white muscle adenylosuccinate synthetase and adenylosuccinase is suggested by the conversion of aspartate into malate during increased energy demand. There is no evidence of ammonia incorporation into alanine, glutamate or glutamine.
...
PMID:Goldfish muscle energy metabolism during electrical stimulation. 661 58

The variations of kinetic parameters with pH of the activity of 14-day-old chicken embryo and adult hen skeletal muscle AMP-deaminase in the presence and in the absence of adenine nucleotide effectors have been examined. The results obtained indicate that the kinetic and regulatory properties of the two developmental forms of AMP-deaminase are different.
...
PMID:Regulatory properties of 14-day embryo and adult hen skeletal muscle AMP-deaminase. The influence of pH on the enzyme activity. 669 89

The variation of kinetic parameters with pH for the reaction catalysed by the purified 14-day embryo and adult hen heart AMP-deaminase was shown to be similar but not identical. The pH-dependence of the half-saturation constant (K0.5) is well pronounced, and the plot of pK0.5 vs pH is manifested as a bell-shaped curve for both developmental forms of the enzyme. In contrast to that, the maximum velocity of the reaction (Vmax) catalyzed by these enzymes does not change significantly in the range pH 5.6-7.4.
...
PMID:Regulatory properties of 14-day embryo and adult hen heart AMP-deaminase; the influence of pH on the enzyme activity. 669 84

Chromatography on phosphocellulose column revealed changes in the elution profile of chicken heart AMP-deaminase during ontogenesis. The extracts from the heart of adult hen and 14 day-old embryo displayed a single peak of the enzyme activity at a slightly different elution volume, whereas in the heart extract of 1 day-old chicken two molecular forms of adenylate deaminase have been eluted. The kinetic and regulatory properties of the purified adult hen heart AMP-deaminase were studied and compared with those of the corresponding enzyme from 14 day-old embryo heart. Both enzymes exhibited a slightly sigmoid-shaped plot of the reaction rate versus substrate concentration, which shifted to hyperbolic form when ATP or ADP were added into the incubation medium. The enzymes were strongly activated by ATP, less efficiently by ADP and the activatory effect was enhanced at low substrate concentration. Orthophosphate inhibited both enzymes but this inhibition was more potent for the embryo heart enzyme. Palmitoyl-CoA inhibited adult hen but not the embryo heart AMP-deaminase. The data presented indicate that the differences also in the regulatory properties of the molecular forms studied do exist and correspond with the ontogenetic differences observed previously (Kaletha and Skladanowski (1981) Experientia 37, 232-234) concerning the effect of temperature on the chicken heart adenylate deaminase.
...
PMID:Regulatory properties of 14 day embryo and adult hen heart AMP-deaminase. 669 90

Interpretation of the kinetic data in terms of concerted transition theory indicated that in the presence of 100 mM potassium chloride hen heart AMP-deaminase may be active as a dimer. The presence of ATP, but not of the ADP in the incubation medium shifts completely the allosteric equilibrium towards the active, accessible to the substrate form of the enzyme. In the joint presence of main enzyme effectors (ATP, ADP and orthophosphate) added to the incubation medium at physiological concentrations, the plot of the reaction rate versus substrate concentration manifested hyperbolic dependence and the value of half-saturation constant (K0.5) did not differ from the value of this parameter obtained for ATP(alone)-activated enzyme.
...
PMID:Hen heart AMP-deaminase--the combined effect of ATP, ADP and orthophosphate on the enzyme activity. 669 91

Adenosine kinase, adenosine deaminase, hypoxanthine phosphoribosyltransferase, inosine-nucleoside phosphorylase, 5'-AMP deaminase and 5'-IMP nucleotidase were identified in cell-free extracts of duckling erythrocytes; no evidence for 5'-AMP nucleotidase and xanthine oxidase activity was found. The Km values for the duckling red cell enzymes were similar to those reported for human erythrocytes. Plasmodium lophurae extracts demonstrated similar enzyme activities except for 5'-AMP deaminase and 5'-IMP nucleotidase which were absent. It is proposed that during infection erythrocytic AMP is catabolized to IMP, inosine and hypoxanthine; the hypoxanthine is taken up by the plasmodium, utilized to form IMP, and this in turn is converted into adenine and guanine nucleotides.
...
PMID:Purine metabolizing enzymes of Plasmodium lophurae and its host cell, the duckling (Anas domesticus) erythrocyte. 678 22

1. Cytosol from pig skeletal muscle, but not heart, contains an inhibitor of AMP-deaminase (AMP-D, EC 3.5.4.6) which reduces AMP-D activity 8-fold. 2. Heart and skeletal muscle AMP-D have been purified to apparent homogeneity by cellulose phosphate and DEAE-Sephacel chromatography. 3. AMP-D from skeletal muscle is inhibited more severely than the heart enzyme by an increase in adenylate energy charge to levels exceeding 0.4. Nevertheless both enzymes seem to be regulated by the energy charge, which contrasts with reports for rabbit heart AMP-D.
...
PMID:Regulation of porcine heart and skeletal muscle AMP-deaminase by adenylate energy charge. 685 80


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

---