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

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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)

Activity of cobalt activated acylase, gamma-glutamyltransferase, leucylaminopeptidase and alanylaminopeptidase in serum and liver of mice with transplantable leukemias (L1210, L1210/ara-C, L1210/CH3-G, AKSL-4, plasmacytoma ADJ-PC-5) were determined. Adenosinotriphosphatase, 5'-nucleotidase and alkaline phosphatase were histochemically localized in lymphatic nodes and spleen. Among the investigated enzymes the rise in serum activity of cobalt activated acylase and gamma-glutamyltransferase was demonstrated. A substantial increase of leucylaminopeptidase and alanylaminopeptidase was shown in the liver. A decrease in the histochemical reactions of all the studied enzymes was observed.
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PMID:Enzyme activity in mice with transplantable leukemia. 287 46

Mice--BDF, hybrides, males aged 3 months were injected intraperitoneally with 10(4) lymphatic leukemia cells P 388. The mice were killed by bleeding after 2.5 and 10 days after the injection. Gamma-glutamyltransferase (GGT), leucylaminopeptidase (LAP) and cobalt activated acylase activity were determined in the serum of the mice. The inner organs of the animals were verified histopathologically. A statistically significant increase in the activity of the examined enzymes was observed together with the development of transplantable leukemia. These enzymes can be helpful in early monitoring of lymphatic leukemia P 388 in mice--as markers of cancer growth.
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PMID:Activity of some hydrolases in mice with transplantable lymphatic leukemia P 388. 288 60

The activity of cobalt-activated acylase was determined in the serum of mice with transplantable leukemia (P 388, L 1210 standard, L 1210/ara-C, L 1210/CH3-G, plasmocytoma ADJPC-5, lymphoma AKSL-4 and natural leukemia in mice NZB). A statistically significant increase in enzyme activity in all leukemias except lymphatic leukemia has been demonstrated. The results suggest possibility of using the enzymatic measurement as a marker of transplantable leukemia in mice.
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PMID:Serum cobalt-activated acylase as a marker of transplantable leukemia in mice. 327 96

AKR mice highly susceptible to leukemia were fed orally for 9 months every days with a water solution of peat-liking preparation PF-290/II/2 at a dose 0.2 cm3 (70 g/cm3 water). After bleeding body and internal organs weight were measured and their ratio were calculated. Anatomo-pathological lesions, histopathological and ultrastructural examinations with the use of transmission and scanning microscope, serum cobalt-activated acylase (AA-Co) activity and urine arylsulphatase (ASA) activity were performed. It was found used preparation had some anti-tumors effect of mice with lymphatic leukemia. Serum cobalt-activated acylase and urine arylsulphatase of AKR mice for observation on disease development and dynamics of this process. In the ultrastructural picture changes of lymphatic cells after outside removal of degradated complexes of intracell membranes was observed.
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PMID:[Morphological and biochemical studies of the effect of the peat-derived preparation PF-290/II/2 on the development of natural lymphatic leukemia in mice]. 348 32

A933 acylase, which is involved in exchange of the pantothenyl substituent of OA-6129 carbapenems with acetyl CoA, was characterized as an L-amino acid acylase with a molecular weight of 100,000 (+/- 8,000) and a pI value of 5.1. The highest L-amino acid acylase activity of A933 acylase was observed at 37 degrees C and pH 7 approximately 7.5 for N-chloroacetyl-L-phenylalanine. Unlike other amino acid acylases, A933 acylase was severely inhibited by cobalt ions and p-chloromercuribenzoate. The acylase also showed peptidase activity with some di- and tripeptides. A protein fraction with A933 L-amino acid acylase activity from blocked mutant 1501 lacked OA-6129A-depantothenylating activity.
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PMID:Studies on the biosynthesis of carbapenem antibiotics. III. Enzymological characterization of the L-amino acid acylase activity of A933 acylase. 401 11

Cells of Bacillus thuringiensis containing refractile spores autolyzed readily when suspended in buffer. The autolysate contained enzymes which lysed vegetative cell walls of the organism. Three enzymes were isolated from the autolysate, and each was purified approximately 30-fold. One enzyme, most active near pH 4.0, was found to be an N-acetylmuramidase. The other two enzymes exhibited pH optima at 8.5. One was stimulated by cobalt ions and the other was not. The cobalt-stimulated enzyme was shown to be an N-acetylmuramyl-l-alanine amidase. The cobalt insensitive enzyme exhibited both N-acetylmuramyl-l-alanine amidase and endopeptidase activity. The amidase activity may reflect incomplete separation of the cobalt-stimulated enzyme. The endopeptidase cleaved the peptide bond between l-alanine d-glutamic acid. A cell wall lytic endopeptidase with this specificity has not been previously reported. All three enzymes were extremely limited in the range of bacterial cell walls which they attacked. Except for cell walls of Micrococcus lysodeikticus, which were lysed by the muramidase, only cell walls of members of the genus Bacillus were attacked.
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PMID:Isolation and characterization of three autolytic enzymes associated with sporulation of Bacillus thuringiensis var. thuringiensis. 573

Cobalt-activated acylase form-2 from human uterine myosarcoma, lung adenocarcinoma and the adjacent tissue was isolated, purified and characterized. It was found, that the enzyme from the malignant neoplasms differed both from the normal tissue and benign tumor acylase-2 in its Km value, temperature optimum and effect of some ions. Some abnormal properties (pH dependence, activation by cobalt and thermostability) were common for benign and malignant tumors. In lung tissue adjacent to adenocarcinoma, some deviations of acylase properties were observed, similar to that found in tumor, indicating that biochemical changes may be present also in tissues unaffected by the neoplastic growth by the histopathological criteria.
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PMID:Abnormalities of cobalt-activated acylase from human sarcoma, carcinoma and the adjacent tissue. 642 3

An intracellular aminopeptidase (alpha-aminoacyl-peptide hydrolase (cytosol), EC 3.4.11.1) isolated from cell extracts of Lactobacillus acidophilus R-26 was purified 634-fold to homogeneity. This enzyme, which was responsible for all of the N-terminal exopeptidase and amidase activities observed in crude extracts, had no detectable endopeptidase or esterase activity. Although a broad range of L-amino acid peptide, amide and p-nitroanilide derivatives possessing free alpha-amino termini are attacked, the enzyme favored substrates with hydrophobic N-terminal R groups. The native enzyme, which was found to be a tetramer of molecular weight 156000, contained 4 mol of tightly bound Zn2+. The catalytically inactive native zinc metalloenzyme was capable of being activated by either Zn2+, Co2+, Ni2+ or Mn2+. The shape of the log Vmax versus pH plot indicates that two active-center ionizable groups (pKES1 = 5.80; pKES2 = 8.00) may be involved in catalysis. Methylene-blue-sensitized photooxidation of the enzyme resulted in the complete loss of activity, while L-leucine, a competitive inhibitor, partially protected against this inactivation. Amino-acid analysis indicated that this photooxidative loss of activity corresponds to the modification of one histidine residue per monomer of protein.
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PMID:Isolation and characterization of an aminopeptidase from Lactobacillus acidophilus R-26. 643 50

A new procedure for the isolation of highly purified acylamino acid amidohydrolase from hog kidney is described which allows the preparation of the enzyme with a recovery of about 45%, a 200 fold purification and a spec. activity of 350-500 U. The essential Zn2+ of the enzyme was exchanged for Co2+, Ni2+, Mn2+ and Cd2+, and the kinetic parameters KM, kcat and kcat/KM of the different enzyme species for a series of acetyl-L-amino acids were determined.
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PMID:[New isolation procedure for swine kidney acylase. Kinetics of Co2+, Mn2+, Ni2+ and Cd2+-enzymes]. 651 35

Aminoacylase (EC 3.5.1.14) from Aspergillus oryzae was purified from a commercially available crude material by heat treatment, precipitation by polyethyleneimine and ammoniumsulfate, gel chromatography and preparative disc-gel-electrophoresis. The purified product was homogenous as judged by polyacrylamide gel electrophoresis. SDS-gel electrophoresis, polyacrylamide-gel-gradient electrohoresis, gel chromatography and amino acid analysis demonstrated the enzyme to be composed of two subunits with Mr of 36 600. The kinetic properties of the enzyme were studied with chloracetyl derivatives of alanine, phenylalanine, methionine, leucine, norleucine and tryptophan. The pH optimum of the acylase activity with chloroacetyl-alanine as substrate is at pH 8.5. Acyl derivatives of hydrophobic amino acids are preferred substrates. The enzyme has no dipeptidase activity. Aminoacylase is not inhibited by SH-blocking agents and no SH-groups could be detected with Ellman's reagent in the native and denatured enzyme. The enzyme activity is insensitive to phenylmethylsulfonyl fluoride and N-alpha-p-tosyl-L-lysine chloromethyl ketone. The microbial acylase is zince metallo enzyme. Mental chelating agents are strong inhibitors; it is further inhibited by Cd2+, Mn2+ and activated by Co2+. The properties of pig kidney and Aspergillus acylase are compared.
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PMID:Aminoacylase from Aspergillus oryzae. Comparison with the pig kidney enzyme. 677 95


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