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)

An enzyme deacylating preferentially N-acyl-L-aromatic amino acids was partially purified from rat kidney. The purification procedure included DEAE-cellulose column chromatography, (NH4)2SO4 fractionation, gel-filtration on a Sephadex G-200 column and further DEAE-cellulose chromatography. The enzyme was thus separated from aminoacylase (N-acylamino-acid amidohydrolase, EC 3.5.1.14) (acylase I). Although the enzyme preparation contained other acylases, the experimental data (effect of p-chloromercuric benzoate, heat stability and inhibition between substrates) suggest that the enzyme acts preferentially on N-acyl derivatives of L-tryptophan, L-tyrosine, L-phenylalanine and L-histidine. This enzyme appears to be present in many animal tissues.
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PMID:N-Acyl-L-aromatic amino acid deacylase in animal tissues. 62 89

The activity of cobalt-activated acylase, measured towards N-chloroacetyl- and N-butyryl-gamma-L-glutamyl-beta-naphthylamide, was found in all tissues of the adult animals. In the kidney, liver and small intestine of adult guinea-pig and rat two fractions differing in electrophoretic mobility (fractions 1 and 2) were present. The early foetus contained fraction 2, sometimes accompanied by fraction 3 which later disappeared; on further development of the foetus, fraction 1 appeared. Fraction 1 was distinctly activated by cobalt ions; fractions 2 and 3 were strongly inhibited by deaminated leucylphenylalanine. In the guinea-pig, the molecular weight of the three fractions ranged from 43000 to 59000.
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PMID:Activity and polymorphism of the cobalt-activated acylase in tissues of rodents during development. 66 76

Newly synthesized and non-toxic acyl derivatives of p-aminobenzoic acid were used as substrates indiagnostic kit for assay of cobalt-activated acylase activity. The enzyme activity, in serum of patients with viral hepatitis, depends on time, type and treatment of the disease and also on age and sex of patients. The presence of HBs antigen has no influence on it. In the patient sera 1-3 molecular forms of the enzyme were found but in the liver of healthy or sick individuals two forms were noted. Using alpha-hydroxy-isocaproyl-tyrosine covalently coupled to Sepharose 4B as a bioadsorbent; the form 2 of acylase from human liver was isolated and separated from the form 1, aminoacylase and aspartyl acylase. Specific immunoglobulins anti-form 2 does not react with other forms of the enzyme either in serum or in the liver.
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PMID:Cobalt-activated acylase in serum of patients with viral hepatitis. 74 9

The role of penicillinacylase in resistance to penicillin of various strains of E. coli differing in the levels of acylase produced was investigated. All the strains produced simultaneously acylase and beta-lactamase. A preparation of pure acylase and an antiacylase immune serum were used in the experiments. The sensitivity testing was accompanied by chromatography of the culture broth with a purpose of finding penicillin inactivation products. A principle possibility of increasing the culture resistance to penicillin under the action of acylase was found. However, in testing the strain sensitivity with a method of serial dilutions the conditions for synthesis and action of acylase were unfavorable. Therefore, the main factor of the culture resistance to penicillin was beta-lactamase and not acylase.
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PMID:[Resistance of acylase-forming strains of E. coli to penicillin]. 77 67

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

The enzymatic synthesis of lysophosphatidic acid, phosphatidic acid, monoacylglycerol and diacylglycerol from sn-[14C]glycerol 3-phosphate occurs in purified chloroplasts. The results indicate that: (1) the chloroplast extract contains a soluble acylase (acyl-CoA: sn-glycerol 3-phosphate acyltransferase); (2) the envelope fraction contains an acyl-CoA synthetase, a bound acylase (acyl-CoA: acyl-sn glycerol 3-phosphate acyltransferase) and a phosphatidic acid phosphatase; without chloroplast extract in the incubation medium, the envelope is unable to incorporate sn-glycerol 3-phosphate into phosphatidic acid and diacylglycerol; addition of chloroplast extract to the incubation medium induced a fast increase of the incorporation of sn-glycerol 3-phosphate into phosphatidic acid and diacylglycerol; thylakoids being unable to incorporate sn-glycerol 3-phosphate (in presence or absence of soluble chloroplast extract in the incubation medium) our results indicate that the envelope of spinach chloroplast is the site of phosphatidic acid and diacylglycerol synthesis; (3) diacylglycerol actively synthesized by the envelope is also the substrate for the first galactosylation enzyme.
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PMID:Site of synthesis of phosphatidic acid and diacyglycerol in spinach chloroplasts. 83 58

It was shown that serum of albino mice infected with plague microbe cells inactivated benzylpenicillin. Such deacetylating activity reached its peak by the 3rd day and after that decreased reaching by the 5th--7th day the level registered in non-infected animal and being apparently of non-specific character. Ampicillin proved to be 2 times more resistant to the effect of serum acylase as compared to benzylpenicillin. It was supposed that the ability of serum of infected animals to inactivate benzylpenicillin by splitting off phenylace acid was the cause of ineffective treatment of experimental plague of albino mice with comparatively low doses of the drug.
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PMID:[Deacylating activity of sera as a cause for the ineffectiveness of the treatment of experimental plaque in white mice with benzylpenicillin]. 84 16

Tryptophan and some indolic metabolites were studied in urine, plasma and dialysate of uraemic patients using thin-layer- and high-pressure liquid chromatography. Some new metabolites: indole-3-carboxylic acid, indole-3-carbaldehyde, indolelactic acid and N-acetyltryptophan were detected. Levels of the latter two metabolites in urine, dialysate and especially plasma suggest increased transamination of tryptophan and a possible defect in renal amino acid acylase in uraemia.
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PMID:Indolic tryptophan metabolism in uraemia. 93 25

Activity of Coiactivated acylase in the serum was investigated in 120 children aged 3 months to 15 years, divided into five age groups, suffering from viral hepatitis (VH). No differences were found in the mean values of acylase activity between the ages of 3 months and 6 years, and progressively rising values in older age groups. Statistical analysis showed significance of the difference between the youngest age group and the group of children aged 12-15 years. A study of the dynamics of acylase activity in the course of the disease in 20 children showed rapidly declining values of this enzyme activity. Presence of HBAg in the serum was demonstrated in 12 children, in whom levels of acylase activity in the serum were similar to those in children without HB antigenemia, but the small number of cases examined does not permit conclusions. Acylase activity increases with age. This enzyme activity was observed in the serum of 96%, and HBAg in 10% of the examined children.
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PMID:Activity of cobalt-activated acylase and Australia antigen (HBAg) in children suffering from viral hepatitis. 96 18

To investigate the metabolic fate of lankacidin C 14-propionate in experimental animals, the 14-C-labeled antibiotic was prepared by the fermentation of Streptomyces rochei var, volubilis in the presence of various 14-C-labeled organic carboxylic acids, amino acids and carbohydrates. Significant incorporation (20 similar to 40%) was observed with L-methionine-methyl-14-C. Lankacidin C 14-propionate-14-C (specific activity 49.6 muCi/mg) was obtained from lankacidin C-14-C and ethyl propionate by the action of an acylase of the streptomyces.
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PMID:Studies on lankacidin-group (T-2636) ANTIBIOTICS. IX Preparation of C-labeled lankacidin C 14-propionate. 112 65


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