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. Preparations of purified pig kidney aminoacylase (N-Acylamino-acid amidohydrolase, EC 3.5.1.14) were obtained by Sephadex and DEAE-cellulose chromatography in homogeneous form as judged by polyacrylamide gel electrophoresis and immunoelectrophoresis. 2. The apparent molecular weight of the enzyme, determined by gel filtration, was about 86 000. After treatment with mercaptoethanol, performic acid or sodium dodecyl sulphate a band with an apparent molecular weight of approximately 43 000 was observed in polyacrylamide gels containing sodium dodecyl sulphate. Thus pig kidney aminoacylase seems to be composed of two subunits. 3. The amino acid composition of the enzyme was determined. Aminoacylase contains 772 amino acids, which corresponds to a molecular weight of 85 500. 12 tryptophan and 12 half-cystine residues were found. 4. Each subunit of the enzyme contains two -SH groups of different reactivity and two disulfide bonds one of which is easily cleaved by -SH compounds, the second only by performic acid oxidation. 5. Chemical modification of two -SH groups abolishes the catalytic activity of aminoacylase. Cleavage of two disulfide bonds also inactivates the enzyme. It is suggested that the enzyme has two active sites each containing an essential -SH group and disulfide bond. One active site is assumed to be part of each subunit.
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PMID:Chemical investigations on pig kidney aminoacylase. 0 49

The authors observed changes in activity of leucine amino-peptidase (E.C. 3.4.1.1--LAP), gamma-glutamyl transpeptidase (F.C 2.3.2.2--GGTP) and Co++-activated acylase in blood serum of patients with ovarian carcinoma, with or without ascites, treated with Ledakrin (1-nitro-9-[3-dimethylaminopropylamino] acridine). It was stated that the activities of LAP and GGTP increased during the treatment and during tumor progression. The level of Co++-activated acylase increased only slightly during the treatment and therefore, the determination of this enzyme appeared to be of no use in monitoring the therapy of ovarian carcinoma.
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PMID:Blood serum peptidases in patients with ovarian carcinoma treated with Ledakrin. 1 75

Co++-activated acylase activity was studied in the blood serum and liver homogenates from rabbits poisoned with CCl4 in doses of 0-5 g/kg body weight intraperitoneally. Activity of this enzyme in serum increased on the first day after poisoning, but the rise was of short duration. Increased serum activity of the enzyme was accompanied by an increase in acylase activity in liver homogenates, which persisted to the ninth day, i.e. to the end of the observation period, when serum acylase activity returned to normal. Co++-activated acylase activity in serum was not correlated with its activity in liver homogenates. Co++-activated acylase activity was significantly correlated with AlAT and GGTP activities, but acylase and LAP were not correlated.
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PMID:Cobalt-activated acylase activity in experimental toxic liver damage. 2 21

A method was elaborated for obtaining polyacrylamide gel zymograms of the cobalt-activated acylase after electrophoresis. Two fractions of the acylase showing activity towards N-chloroacetyl-gamma-L-glutamyl-beta-naphthylamide were found in human kidney, liver and intestine. The two fractions isolated from liver differ in substrate specificity, heat resistance, response to metal ions, inhibition by deaminated dipeptides, and in molecular weight. They differ also from other N-acylamino acid amidohydrolases: aminoacylase (EC 3.5.1.14) and aspartoacylase (EC 3.5.1.15).
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PMID:Polymorphism of the cobalt-activated acylase in human tissues. 2 51

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

The acylase activity was studied with 65 cultures of mycophilic fungi belonging to 56 species and 33 genera. Among these: 9 species displayed the acylase activity toward ampicillin; 8 species, toward phenoxymethylpenicillin; 6 species, toward benzylpenicillin; and 21 species manifested the complex activity. Many of the active species belonged to the bionecrotrophic group of mycophilic fungi, the number of necrotrophic fungi was less, while that of biotrophs and saprotrophs was even lower.
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PMID:[Acylase activity of mycophilic fungi]. 9 1

The production of high fructose corn syrups was greatly facilitated by the use of immobilized glucose isomerase. Similarly, in Japan, the fermentation industry proved its processing efficiency for amino acids through the use of immobilized amino acid acylase. This article discusses the use of soluble enzymes in the food industry followed by a section on the various available methods to immobilize enzymes. Once enzymes are immobilized, many of their operational parameters could be altered. Rationale for the determination of the effects of immobilization is provided. A relatively new concept is the use of a single matrix for immobilizing more than one enzyme. Immobilized multi-enzyme systems offer many attractive advantages; however, such a process also raises some interesting questions about kinetics. These questions and their suggested answers are discussed in the penultimate section. The major emphasis of this article is on the use of immobilized enzymes in the food industry. Two systems--amino acylase and glucose isomerase--have been demonstrated to be techno-economically feasible. Immobilization of other enzymes, such as glucoamylase, lactase, protease, and flavor modifying enzymes, has received some attention. The potential of these new systems are also discussed.
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PMID:The use of immobilized enzymes in the food industry: a review. 11 2

The products of penicillinase and acylase hydrolysis of benzylpenicillin were studied with a method of sorbent thin-layer chromatography. The method provided qualitative determination and differentiation of penicillinase and acylase activity in cultures of E. coli capable of simultaneous production of both enzymes. It was shown that when the cultures of E. coli were grown under conditions optimal for acylase production, the amounts of penicillinase were insignificant.
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PMID:[Determination of penicillinase and acylase by chromatography on a thin layer of sorbent in the case of their joint formation by different strains]. 16 9

The synthesis of benzylpenicillin and 6-aminopenicillanic acid, labeled with tritium in the beta-methyl group, is described. Benzylpenicillin S-sulfoxide benzyl ester is refluxed in benzene and tritiated water and is successively debenzylated and deoxygenated to (beta-methyl-3H)-benzylpenicillin. Removal of the side chain with a bacterial acylase gives (beta-methyl-3H)-6-aminopenicillanic acid.
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PMID:Synthesis of (beta-methyl-3H-)-benzylpenicillin and (beta-methyl-3H)-6-aminopenicillanic acid. 17 70

Amino acid analysis on the acid hydrolyzate of polymyxin S1 revealed its amino acid composition. Isolation of the constituent amino acids and measurement of their optical activities clarified their chiralities: Dab(5L), Thr(3L), Ser(1D) and Phe(1D). The constituent fatty acid was identified with anteisononanoic acid by gas chromatography and mass spectrometry. By the action of polymyxin acylase, deacyl polymyxin S was obtained. Successive EDMAN degradation reaction on deacyl polymyxin S revealed the amino acid sequence. Further evidence for the structure of polymyxin S1 was obtained by partial acid hydrolysis on tetra-(DNP)-polymyxin S1.
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PMID:The structure of polymyxin S. (Studies on antibiotics from the genus Bacillus. XXI). 20 83


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