Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Kinetic data for avian erythrocyte AMP-deaminase in lysate supernatants and 2000-fold purified enzyme were consistent with an allosteric model having four binding sites for substrate. 2. Relative to the purified enzyme, AMP-deaminase in lysate supernatants exhibited a greater S0.5 and enhanced sensitivity toward phytic acid, but was far less sensitive toward potassium ion. 3. In the absence of potassium chloride, the enzymatic activity in lysates exhibited hysteresis at subsaturating 5'-AMP. This response was modified reversibly by allosteric ligands. 4. It is concluded that the characteristics of avian RBC AMP-deaminase, as expressed in lysates, may reflect important intermolecular interactions and better represent the regulatory properties of this enzyme in erythrocytes.
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PMID:Regulation of avian erythrocyte AMP-deaminase. 4 52

1. Michaelis constants, maximum velocity and pH-dependence of the reaction catalysed by homogeneous AMP-deaminase preparations from hen, frog and pikeperch skeletal muscle were compared, as well as the influence of monovalent cations, ATP and inorganic phosphate. 2. ATP was found to activate the enzymes in the absence of K+ and at optimum (150 mM) KCl concentration. 3. Absolute dependence on potassium ions and considerable dependence of Km and Vmax on the kind of monovalent cation present in the medium were found for pikeperch enzyme.
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PMID:Comparative studies on muscle AMP-deaminase--II. Regulation by monovalent cations, ATP and orthophosphate of the enzyme from hen, frog and pikeperch muscle. 4 54

Strains of Geotrichum candidum were isolated from the surface of a commercial sample of Limburger cheese and from raw milk. Growth of the isolates in an acidified tryptone-yeast extract medium was accompanied by a rise in the pH of the medium from 3.5 to above 7.0 Ammonia production, as indicated by Nesslerization, was associated with the deamination of glutamic and aspartic acids. The first reaction in the production of ammonia from glutamic acid, isomerization to beta-methylaspartic acid, required vitamin B12 and the second reaction, the deamination of beta-methylaspartic acid to mesaconic acid and ammonia, was dependent on magnesium and potassium. The conversion of aspartic acid to fumaric acid and ammonia required magnesium. These minerals were in sufficient amounts in the Limburger cheese for optimum deaminase activity.
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PMID:Deamination of glumatic and aspartic acids by Geotrichum candidum. 58 76

The quantitative method for determination of penicillinacylase activity is described. The method is based on detection of phenylacetic acid (PAA) formed during hydrolysis of benzylpenicillin. PAA is extracted with toluol and nitrated with potassium nitrate solution in concentrated sulphuric acid followed by reduction of nitrophenylacetic acid into aminophenylacetic acid with zinc powder. Aminophenylacetic acid interacts with p-dimethylaminobenzaldehyde in acid medium forming a coloured compound (Schiff base). The optic density of the latter was determined with spectrophotometer SF-16 at 430 nm. The method was used for determination of acylase in Yersinia species and some other bacteria.
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PMID:[Method for the quantitative determination of penicillin acylase activity by the formation of phenylacetic acid]. 79 10

Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single badn on starch and polycrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B 10-Gel P-100, gave values of 40 000 +/- 4 000. Data obtained suggest that cow liver deaminase exists as a single polypeptide chain. Heating partially purified preparations of deminase resulted in an enhancement of activity. Added cosynthetase to these fractions increased the percentage of uroporphyrinogen III formed but also diminished total uroporphyrinogens synthesis. The action of several compounds added to the system was studied. Thiol reagents and divalent metals as Hg 2+ , Pb2+, (d2+ and Zn2+ inhibited deaminase, indicating the presence of thiol groups essential for activity, probably involved in the cyclization step. Certain concentrations of sodium, potassium and magnesium salts enhanced activity. Several chelators tested were without effect on the deminase. Some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited the enzyme.
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PMID:Studies on cow liver porphobilinogen deaminase. 105 1

Angiotensin II has been found to stimulate 5'-adenylic acid deaminase from rabbit skeletal muscle. Stimulation was discernible around 10(-9) M and peak stimulation of about threefold was seen at 10(-7) M, concentrations approximating those required for stimulation of vascular smooth muscle or adrenal glomerulosa cells. Higher concentrations produced less stimulation. Adenosine triphosphate stimulated to the same degree, but a concentration of 10(-5) M was required for maximum stimulation, while maximum stimulation with sodium or potassium required 0.5 M and 0.75 M, respectively. Although the physiologic significance of these observations has not been established, these data suggest an intracellular role for angiotensin II.
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PMID:Angiotensin II stimulation of 5'-adenylic acid deaminase. 125 Aug 47

The effects of various commercial and model surfactants of different structure and hydrophilicity were studied on water-in-oil (w/o) emulsion stability, potassium cation leakage and permeation of 6-nitro-3-phenylacetamide benzoic acid in a model system using Penicillin acylase (EC 3.5.1.11) immobilized in a liquid membrane. Both emulsion stability, potassium leakage and permeation of organic substances depend upon hydrophilicity of surfactants. Hydrophilic surfactants may be used to stabilize emulsions only in mixtures with hydrophobic emulsifiers. Additions of small quantities of hydrophilic surfactants to the system in which permeation occurs together within an enzymatic process may be advantageous. Both the rate of permeation and potassium transfer significantly increase when hydrophilic surfactants are present. There was no relationship observed between potassium cation transfer from the internal phase and emulsion stability in the storage test.
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PMID:Permeation of 6-nitro-3-phenylacetamide benzoic acid (NIPAB) and hydrolysis by penicillin acylase immobilized in emulsion liquid membranes. 136 99

Intact cells Escherichia coli CCM 2843, exhibiting substantial benzylpenicillin amidase activity, were bound mutually with supporting waste microbial cells, native or treated, to obtain an inexpensive biocatalyst for the production of 6-aminopenicillanic acid (6-APA). The bond was effected by glutaraldehyde (GA) and Sedipur CL-930 (PEI), without any carrier. The optimal concentration of GA was 2%, that of PEI 1%. The optimal biocatalyst was obtained by immobilization of productive cells with their fragments at a mass ratio of 4:1. The cell aggregates were used for hydrolysis of potassium benzyl-penicillin at a concentration of 5% to 6-APA. After 25 repeated batch conversions the degree of conversion did not decrease; its average value was 96.4%.
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PMID:Cell aggregates of Escherichia coli with benzylpenicillin amidase activity. 182 39

Penicillin acylase (EC 3.5.1.11) was completely inactivated with equimolar phenylmethane [35S]sulphonyl fluoride (PhMe35SO2F); the stability of the sulphonyl group in the modified protein was determined by measurement of the radioactivity in ultrafiltrates. In 8 M urea, the rate of loss of the sulphonyl group was similar to that observed in PhMeSO2F-inactivated chymotrypsin [Gold, A.M. & Fahrney, D. (1964) Biochemistry 3, 783-791]. Incubation of the PhMeSO2F-inactivated acylase with 0.7 M potassium thioacetate yielded an acetylthiol enzyme which was subsequently converted to a thiol-enzyme during incubation with 10 mM 6-aminopenicillanic acid. 4-Pyridyl-ethylcysteine was released by acid hydrolysis after reaction of the thiol-protein with 4-vinylpyridine. The rates of reaction of thiol-penicillin acylase with iodoacetic acid and 2,2'-dipyridyl disulphide were consistent with the presence of an incompletely accessible cysteinyl sidechain. After carboxymethylating the thiol-enzyme with iodo[2-3H]acetic acid, the label was shown by SDS/PAGE and sequencing analysis to be associated exclusively with the beta-chain NH2-terminal residue, indicating conversion of Ser290 to S-carboxymethyl-cysteine. Near-ultraviolet CD spectra showed the conformation of thiol-penicillin acylase to be indistinguishable from that of the native protein but the catalytic activity was less than 0.02% of that of the normal enzyme. The possibility that Ser290 acts as a nucleophile in catalysis is discussed.
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PMID:Site-directed chemical conversion of serine to cysteine in penicillin acylase from Escherichia coli ATCC 11105. Effect on conformation and catalytic activity. 184 24

AMP-deaminase from human uterine smooth muscle has been isolated, and properties of the enzyme were characterized. At pH 7.0, and in the presence of 100 mM potassium chloride the enzyme manifests a distinctly sigmoidal type of kinetics, with S0.5 parameter value about 12 mM. 1 mM ATP strongly activates the enzyme, and diminishes the value of S0.5 to 1.2 mM. In contrast to that 2.5 mM orthophosphate slightly inhibits the activity of AMP-deaminase studied and increases the S0.5 to about 14 mM. Similarly to ATP, orthophosphate does not influence the maximum velocity of the reaction. Electrophoresis in the presence of sodium dodecyl sulphate revealed that the molecular weight of human smooth muscle AMP-deaminase subunit is close to 37 kDa.
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PMID:Purification and properties of AMP-deaminase from human uterine smooth muscle. 201 70


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