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)

The effect of chemical modification on the acetylcholinesterase and the aryl acylamidase activities of purified acetylcholinesterase from electric eel and basal ganglia was investigated in the presence and absence of acetylcholine, the substrate of acetylcholinesterase, and 1,5-bis[4-(allyldimethylammonium)phenyl]pentan-3-one dibromide (BW284C51), a reversible competitive inhibitor of acetylcholinesterase. Trinitrobenzenesulfonic acid, pyridoxal phosphate, acetic anhydride, diethyl pyrocarbonate, and 2-hydroxy-5-nitrobenzyl bromide under specified conditions inactivated both acetylcholinesterase and aryl acylamidase in the absence of acetylcholine and BW284C51. Chemical modifications in the presence of acetylcholine and BW284C51 by all the above except diethyl pyrocarbonate selectively prevented the loss of acetylcholinesterase but not aryl acylamidase activity; modification by diethyl pyrocarbonate in the presence of acetylcholine and BW284C51 prevented the loss of both acetylcholinesterase and aryl acylamidase activities. Treatment with N-acetylimidazole resulted in the inactivation of acetylcholinesterase and the activation of aryl acylamidase. These changes in both the activities could be prevented by acetylcholine and BW284C51. Modification by phenylglyoxal, 2,4-pentanedione, or N-ethylmaleimide did not affect the enzyme activities. Indophenylacetate hydrolase activity followed a pattern similar to that of acetylcholinesterase in all the above modification studies. The results suggested essential lysine, tyrosine, tryptophan, and histidine residues for the active center of acetylcholinesterase and essential lysine, histidine, and tryptophan residues for the active center of aryl acylamidase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chemical modification of acetylcholinesterase from eel and basal ganglia: effect on the acetylcholinesterase and aryl acylamidase activities. 638 42

An enzyme responsible for the deacylation of beta-citryl-L-glutamate to citrate and glutamate has been characterized in rat testis. The enzyme required manganese ion for full activity and was strongly inhibited by nucleotides such as ATP or GTP. The activity was localized in the particulate fractions. The enzyme favored N-formyl-L-glutamate greater than beta-citrly-L-glutamate greater than beta-citryl-L-glutamine in a decreasing order. The amidohydrolyase activity was highest in the testis and lung, a moderate activity was detected in heart, kidney and intestine, and low in brain, thymus, stomach, skeletal muscle, spleen and liver. These findings suggest that the amidohydrolase is different from any of amidohydrolases reported so far, amidohydrolase I (EC 3.5.1.14), II (EC 3.5.1.15), III, N-acetyl-lysine deacylase (EC 3.5.1.17) and N-acetyl-beta-alanine deacetylase (EC 3.5.1.21), and various peptidases.
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PMID:A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes. 641 21

he methods for detecting two activities, i. e. lysine amidase and alpha-aminocaprolactam hydrolase ones, in crude extracts of Cryptococcus sp. are described. The method for registering lysine amidase activity is based on the ability of Cu(II) complex to absorb at 230 nm. The products of lysine and alpha-aminocaprolactam interactions with o-phthalaldehyde in the presence of mercaptoethanol possess different molar absorption at 340 nm. This fact was used for detecting alpha-aminocaprolactam hydrolase activity. The main merit of the methods is the possibility to register the data on the course of the reaction without preliminary chromatographic separation of the reaction products and reactants. The methods proposed do not require expensive enzymes, such as lysine decarboxylase and lysine-alpha-ketoglutarate-epsilon-aminotransferase, which are used for the quantitative estimation of lysine.
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PMID:[Determination of lysine amidase and alpha-aminocaprolactam hydrolase activities in cell-free extracts of Cryptococcus sp]. 642 Jul 86

Peptidoglycan (PG)-polysaccharide (PS) polymers derived from group A streptococcal cell walls were solubilized by M-1 mutanolysin (endo-N-acetylmuramidase) and phage-associated lysin (N-acetylmuramyl-l-alanine amidase). Fragments were isolated by ultrafiltration and a series of gel filtrations and were injected intravenously into Sprague-Dawley rats. No fragments with a molecular weight of less than 5 x 10(6) were able to induce arthritis by systemic injection. However, the enzyme-derived fragments displayed a new biological activity. High-molecular-weight PG-PS fragments ( congruent with500,000) derived from mutanolysin digests induced a severe edematous reaction in the front and hind limbs. The response started 5 to 10 min postinjection, reached maximum intensity in approximately 30 min, and disappeared by 10 h. The smallest dose capable of eliciting the response was 0.31 mug/g of body weight. Low-molecular-weight PG-PS ( congruent with30,000) derived from the mutanolysin digests and the PG-PS fragments isolated from phage-associated lysin digests also induced edema; however, a higher dose was required to elicit the same response as that produced by high-molecular-weight PG-PS fragments. The active fragments contained rhamnose, glucosamine, muramic acid, alanine, glutamic acid, and lysine in various molar ratios. PG-PS fragments obtained by sonic degradation of cell walls (molecular weight >/=5.3 x 10(6)), as well as enzyme-treated PG preparations and muramyl dipeptide, failed to elicit the response. These findings indicate that PG-PS fragments of sizes too small to be arthritogenic can affect the vascular endothelium to induce a rapidly developing edema. Fragments with this biological property could have a key role in the pathogenesis of experimental arthritis by influencing the tissue distribution of arthritogenic PG-PS.
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PMID:Soluble peptidoglycan-polysaccharide fragments of the bacterial cell wall induce acute inflammation. 675 2

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

The collagenolytic serine protease (crab protease) isolated from the hepatopancreas of the fiddler crab, Uca pugilator, has been investigated with respect to its peptide bond specificity and catalytic properties by using noncollagenous substrates. In contrast to vertebrate collagenases, crab protease is a good general protease capable of degrading a variety of polypeptide and synthetic low molecular weight substrates. Crab protease displays a broad range of specificity, cleaving on the carboxyl-terminal side of residues with both positively and negatively charged side chains as well as hydrophobic side chains. The enzyme appears to favor tyrosyl, phenylalanyl, leucyl, and perhaps lysyl residues and, to a lesser extent, arginyl and glutamyl residues. The rate of cleavage of polypeptide substrates is similar to chymotrypsin but is significantly less than trypsin or chymotrypsin for low molecular weight esterase and amidase substrates. Crab protease is effectively inhibited by chymostatin but not by leupeptin or elastatinal. Several common chloromethyl ketone derivatives of phenylalanine and lysine are also ineffective, although crab protease efficiently cleaves at these residues in polypeptide substrates.
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PMID:Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates. 678 31

After partial reduction of disulfide bonds in the thaumatins, the sweet-tasting proteins from the fruits of Thaumatococcus danielii Benth, a rapid autodigestion was demonstrated. In the presence of suitable substrates, the reduced thaumatins showed protease, amidase and esterase activity. Thiol-blocking reagents like mercury(II) chloride inhibited the enzymatic activity. Of the thaumatins b, c, I, II and III (with increasing isoelectric points), thaumatin I showed the lowest enzymatic activity. In this series, the enzymatic activity increased from thaumatin I to thaumatin III as well as from thaumatin I to thaumatin b. Acetylation of the epsilon-amino group of lysine residues in the thaumatins by acetic anhydride, causing a decrease in basicity, led to an increase in enzymatic activity, which is correlated with the number of acetyl groups introduced. Comparison of the amino acid sequence of thaumatin I with that of cysteine proteases of plant origin showed no similarities. Moreover, the thaumatins lack histidine, one of the amino acids in the active site of the cysteine proteases. Monellin, the sweet-tasting protein from the fruits of Dioscoreophyllum cumminsii Diels, is not enzymatically active. However, when monellin with acetylated epsilon-amino groups of lysine residues was brought into a reducing environment it appeared to be enzymatically active. The similarities in properties of the thaumatins and monellin suggest a structural relationship between these proteins.
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PMID:Enzymatic properties of the sweet-tasting proteins thaumatin and monellin after partial reduction. 698 15

Lipoglycans (previously designated lipopolysaccharides) from several species of Acholeplasma and from Thermoplasma acidophilum were examined for endotoxin-like activities as measured by the standard rabbit fever test and the Limulus amoebocyte lysate assay. The lipoglycans from Acholeplasma granularum, Achloplasma laidlawii, Acholeplasma modicum, and Acholeplasma oculi caused a febrile response at concentrations of 1 ng/ml per kg or greater, whereas with control Escherichia coli EC-2 lipopolysaccharides, 6.25 ng/ml per kg was required. Similar results were obtained in the Limulus amoebocyte lysate test. The minimum concentrations in nanograms per milliliter required to stimulate formation of a solid clot were: Acholeplasma axanthum, 0.22; A. granularum, 0.85; A. modicum, 0.51; A. laidlawii, 1.05; A. oculi, 0.74. Standard E. coli 1B lipopolysaccharide required a concentration of 0.125 ng/ml. Thermoplasma lipoglycan was least active, requiring 4.25 ng/ml. Clotting of the Limulus lysate proceeds by the activation by lipopolysaccharide plus Ca(2+) of a proenzyme which cleaves an arginine-lysine peptide bond of the coagulogen. The clotting and amidase activities are inactivated by deoxycholate and can be reactivated by addition of lipopolysaccharide and Ca(2+). As with E. coli 1B lipopolysaccharide, acholeplasmal lipoglycans were shown to restore both clotting and amidase activities of the deoxycholate-inactivated Limulus clotting enzyme. The degree of restoration of amidase activity by mycoplasmal lipoglycans relative to E. coli lipopolysaccharide (1.00) were: A. axanthum, 1.71; A. modicum, 1.22; A. granularum, 0.61; and Thermoplasma, 0.37. The coagulating enzyme, restored with either E. coli lipopolysaccharide or mycoplasmal lipoglycans, was able to react with the synthetic peptide benzoyl-Ile-Glu-(gamma-OCH(3))-Gly-p-nitroaniline (an analog of the coagulogen) or with the purified coagulogen itself to form the clot. The mycoplasmal lipoglycans alone were incapable of promoting these reactions when incubated with the synthetic peptide or with the purified coagulogen, thereby ruling out the contamination of these lipoglycans with proteases capable of cleaving the same Arg-Lys peptide bond of the coagulogen. These results show that acholeplasmal lipoglycans possess endotoxin-like activities. Their passive or active role in disease remains to be established.
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PMID:Endotoxin-like activities of mycoplasmal lipopolysaccharides (lipoglycans). 742 42

Allantoate amidohydrolase from Bacillus fastidiosus was purified 170-fold to homogeneity as judged by isoelectric focusing and nondenaturing and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass was estimated to be 128 kDa. The enzyme appeared to be a homodimer with a subunit molecular mass of 66 kDa. The enzyme has an isoelectric point of 5.6. Allantoate amidohydrolase is a Mn(2+)-dependent enzyme exhibiting a pH optimum around 8.8. Its Km value for allantoate was estimated to be 9 mM. Similar to other microbial allantoate amidohydrolases the enzyme can be reversibly activated and inactivated. No indication for the involvement of arginine, lysine, and cysteine residues in the catalytic action of the enzyme was obtained. Diethylpyrocarbonate strongly inhibited the enzyme activity, indicating the involvement of histidine or tyrosine residues in catalytic action. However, no recovery was obtained by treatment with hydroxylamine as would be expected if such residues were modified. The enzyme could be reversibly denatured by urea, guanidine, and sodium dodecyl sulfate.
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PMID:Purification and characterization of allantoate amidohydrolase from Bacillus fastidiosus. 750 67

Polymyxin acylase isolated from Pseudomonas sp. M-6-3 was used as an N-myristoyl cleaving enzyme in order to determine a part of the N-terminal amino acid sequence of N-myristoyl proteins. The enzyme hydrolyzed a number of N-myristoyl oligopeptides at various hydrolysis rates but not N-myristoyl proteins. The oncogenic protein (N-myristoyl-pp60c-src) was isolated from human colon adenocarcinoma cell line COLO 320DM by two-dimensional polyacrylamide gel electrophoresis. The protein was digested with trypsin and the resultant tryptic N-myristoyl tetrapeptide (N-myristoyl-Gly-Ser-Asn-Lys) was purified by HPLC and the structure was determined both by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI TOF MASS) and by a gas-phase protein sequencer before or after treatment with the polymyxin acylase. The results suggest that the N-myristoyl peptide sequence derived from N-myristoyl proteins was clearly determined by the combined use of MALDI TOF MASS and the N-myristoyl cleaving enzyme.
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PMID:Determination of N-myristoyl peptide sequence both by MALDI TOF MASS and with an N-myristoyl cleaving enzyme (polymyxin acylase). 750 45


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