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)

The immobilization of aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.14) was investigated by using tannin immobilized on aminohexyl cellulose. The most active immobilized aminoacylase was obtained when aminoacylase was adsorbed to the immobilized tannin in a weak alkaline medium containing sodium chloride and n-butanol at 37 degrees C. The activity of the immobilized tannin-aminoacylase complex per unit volume was five times higher than that of the DEAE-Sephadex-aminoacylase complex used for industrial production of L-amino acids in our plants. The half-life of the immobilized tannin-aminoacylase complex was 20 days under continuous operation at a high concentration of substrate; on the contrary, that of the DEAE-Sephadex-aminoacylase complex was 0.5 days.
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PMID:Immobilization of aminoacylase by adsorption to tannin immobilized on aminohexyl cellulose. 3 48

Extracts containing penicillin acylase were obtained by shaking the mycelium of Fusarium avenaceum and of Penicillium chrysogenum in 0.2 M sodium acetate or sodium chloride solution. The optimum pH for conversion of penicillin V into 6-aminopenicillanic acid (6-APA) by the enzyme of Fusarium was about 7.5, and the reaction velocity was increased by a rise in temperature from 27 to 37 C. Penicillin G and penicillins with an aliphatic side chain were cleaved much less readily than was penicillin V. With the enzyme preparation obtained from a nonpenicillin-producing strain of P. chrysogenum, the reaction rate was higher at pH 8.5 than at pH 7.5 and pH 6.5. The acylase of P. chrysogenum hydrolyzes penicillin V more readily than penicillin G. In a series of aliphatic penicillins, the amount of 6-APA formed through the action of this enzyme increased with the number of carbon atoms of the side chain. Penicillins with a glutaryl or an adipyl group as side chain were unaffected by the enzyme of Fusarium and of Penicillium. No reaction was observed upon incubation of penicillin N (with a D-aminoadipyl side chain) or isopenicillin N (with an L-aminoadipyl side chain) with Fusarium and Penicillium extract. When the carboxy group of the side chain of these penicillins was esterified, formation of 6-APA was observed upon incubation with Penicillium extract, whereas no 6-APA or only very small amounts were obtained by acylase of Fusarium.
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PMID:Specificity of penicillin acylase of Fusarium and of Penicillium chrysogenum. 497 22

Penicillin acylase of E. coli NCIM 2400 has been purified to homogeneity using a combination of hydrophobic interaction chromatography and DEAE-cellulose treatment. A variety of substituted matrices were synthesized using D- or DL-phenylglycine, norleucine, ampicillin, or amoxycillin as ligands, all of which retained penicillin acylase at high concentrations of ammonium sulfate or sodium sulfate. The enzyme could be eluted nonbiospecifically by buffer of lower ionic strength with over 95% recovery of the activity. Ammonium chloride, ammonium nitrate, sodium chloride, sodium nitrate, and potassium chloride were ineffective in either adsorption or elution of the enzyme on these columns. Further purification of this partially pure enzyme with DEAE-cellulose at pH 7.0-7.2 yielded an enzyme preparation of very high purity according to electrophoretic and ultracentrifugal analyses, its specific activity being as high as 37 U/mg protein. The purified enzyme has a molecular weight of 67,000 a sedimentation coefficient of 4.0S, and resolves into two forms upon isoelectric focusing. Overall recoveries ranged between 75 and 85%. Ease of operation, high recoveries, high purity of the enzyme and prolonged reuse of the conjugates make the process economically feasible and possibly of great commercial importance.
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PMID:Novel approaches to the purification of penicillin acylase. 639 70

During adaptation of barley (Hordeum vulgare L.) seedlings to extremely high concentrations of sodium chloride in the root space, the content of galactolipids of chloroplast membranes decreased considerably. Alterations in membrane lipids were due to the high concentration of ions rather than to the increase in the water potential. Sodium chloride was accumulated in the leaf cells and affected lipid-synthesizing enzymes such as galactosyl transferase and acylase which are attached to the chloroplast envelope. The return of salt-adapted barley seedlings to a nutrient solution with low salt concentration resulted in a reversal of the observed changes. It is suggested that the decrease in content of galactolipids in biomembranes is one of the factors causing increased salt resistance in barley plants which are adapted to extreme salinity.
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PMID:Changes in Chloroplast Membrane Lipids during Adaptation of Barley to Extreme Salinity. 1666 May 10

The use of sodium chloride to melt highway and road snow is believed to have a significant effect on the groundwater ecosystem of the rivers where the salt from the roads drain. As the river composition changes, the bacterial population also changes to favour those bacteria that are more suited to the higher salt concentrations. In this experiment, we surveyed the cultivable salt-loving organisms (halophiles) on three sites that encompass the Rouge River (Lotz; site 1, Lilly, site; 8, and Ford Field, site 9). A total of 125 isolates were surveyed. Representative isolates of distinct morphologies were subjected to physiological test, using API strips and identified by 16 rDNA sequence analysis. The 16S rDNA sequences were analyzed and compared with sequences from Genbank. Results indicated that the SSU rRNA sequences of the bacterial isolates were similar to six major genera, Bacillus, Staphylococcus, Halobacillus, Paenabacillus, Halomonas, and Clostridium. Half of the isolates sequenced were similar to Bacillus spp. The API assay showed that the majority of the isolates were positive for the enzymes tryptophane deaminase, gelatinase and beta-galactosidase. Indole production, acetoin production and citrate utilization were not observed for any isolates. Fermentation of carbohydrates was observed for very few isolates. The primary enzyme found in all isolates was arginine dihydrolase, which might be an indicator of the presence of such enzyme in halophilic and halotolerant bacteria present in the Rouge River.
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PMID:Halophilic and halotolerant bacteria from river waters and shallow groundwater along the Rouge River of southeastern Michigan. 1743 82