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 three enzyme activities, carboxylesterase, aryl acylamidase and cholinesterase activities, have been found in rat and human sera. Rat serum carboxylesterase associated with serum aryl acylamidase activity, but not with serum cholinesterase activity, was purified by ammonium sulfate precipitation, followed by successive chromatographies on DEAE-cellulose, blue Sepharose and QAE-Sephadex, and then electrophoresis. Evidence for the identity of the two enzymes, carboxylesterase and aryl acylamidase, was their co-elution profiles and co-purification in the different steps, including electrophoresis, with constant ratios of specific activities and percentage recoveries. Human serum carboxylesterase associated with serum cholinesterase, purified earlier, was compared with the rat serum esterase. Human serum carboxylesterase and aryl acylamidase activities were inhibited by serotonin and neostigmine, whereas rat serum carboxylesterase and aryl acylamidase activities were not affected by these compounds. Tyramine activated human but not rat aryl acylamidase. Rat and human serum esterase activities were both strongly inhibited by the diisopropylfluorophosphate. Both esterases catalyzed the hydrolysis of short-chain triacylglycerols, such as tributyrin, and medium-chain monoacylglycerols, such as monocaprin, but not the hydrolysis of long-chain triacylglycerols.
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PMID:Carboxylesterases in rat and human sera and their relationship of serum aryl acylamidases and cholinesterases. 685 27

A 4-methylene-L-glutamine amidohydrolase has been partially purified from leaf extracts of 2-week germinated peanuts (Arachis hypogaea). Purification steps include DEAE-Sephacel and gel filtration chromatography as well as chromatofocusing; amidohydrolase purified 300- to 400-fold is obtained. The enzyme has an approximate molecular weight of 45,000 as determined by gel filtration chromatography and polyacrylamide gel electrophoresis, a broad activity optimum between pH 8.0 and 9.0, and is highly specific toward 4-methylene-L-glutamine. Of a number of amides tested as substrate, only L-glutamine serves 20% as effectively as the methylene-substituted analog. Multiple bands of activity, seen when enzyme samples are electrophoresed on polyacrylamide gels, are not completely resolved but appear to be very similar in molecular weight, pK values, and subcellular localization. Activity is not affected either by added thiols, metal ions, sulfhydryl-reacting reagents, or metal-ion chelators; it is inhibited by borate ions but stimulated by sodium dodecyl sulfate. This amidohydrolase activity is absent in imbibed seeds, but on germination increases rapidly in the cotyledons and leaves for 3 weeks followed by a gradual decline as the plant matures. Activity is almost completely (95%) localized in the leaves and cotyledons. Differential centrifugation studies indicate that the enzyme is found solely in the soluble fraction of peanut leaves.
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PMID:Purification and properties of a 4-methylene-L-glutamine amidohydrolase from peanut leaves. 686 6

1. Two fractions of aryl acylamidase (EC 3.5.1.13) were further separated from rat brain extracts at pH 7.5 by ammonium sulfate precipitation and Bio-Gel chromatography. 2. 1,2,3,4-Tetrahydro-beta-carboline competitively inhibited (67%) fraction-1 but slightly inhibited (13%) fraction-2. Tetrahydroharman, 6-hydroxy-tetrahydroharman and harminic acid slightly inhibited both fractions. Harmalol inhibited fraction-1 but enhanced fraction-2. 6-Methoxy-harman, 6-methoxy-harmalan and harmaline enhanced both fractions. 3. Pargyline did not affect either fraction. Methiothepin, cyproheptadine and chlorimipramine inhibited fraction-1 but stimulated fraction-2. 4. Neostigmine moderately (30%) inhibited AAA-2 but did not have any significant effect on AAA-1. 5. These results indicate that the beta-carboline compounds might play a role in regulating activity of AAA-1 and 2 in brain. 6. Both fractions might be related to serotonergic neurons but only AAA-2 might be associated with acetylcholinesterase.
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PMID:Rat brain aryl acylamidase: further characterization of multiple forms. 710 57

Formiminotransferase-cyclodeaminase, an octameric protein of identical, bifunctional polypeptides of Mr = 62,000, yields a transferase-active fragment of Mr = 80,000 upon proteolysis with chymotrypsin in the presence of the inhibitor folic acid. The purified fragment contains one size of polypeptide, Mr = 39,000, on dodecyl sulfate gels. Cross-linking with the bifunctional reagent dithiobis(succinimidyl propionate) confirmed the dimeric structure of the purified fragment. Reaction of the native octamer with the very short bifunctional reagent difluorodinitrobenzene yields dimer and tetramer in excess of trimer, thereby indicating two types of subunit interaction in the protein. The isolation of a dimeric fragment after proteolysis and the results of cross-linking support a tetramer of dimers structure for the native enzyme. The purified transferase fragment has approximately 68% of the activity of the native enzyme, but has lost specificity for the naturally occurring polyglutamate derivatives of tetrahydrofolate. This is illustrated by an increase in Km for tetrahydropteroylpentaglutamate from 3.4 microM with the native transferase to 89 microM with the fragment transferase. It is suggested that the bifunctional enzyme may have only one polyglutamate binding site/pair of transferase-deaminase sites.
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PMID:The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers. 741 Apr 36

L-Amino acid acylase and D-amino acid acylase of Pseudomonas sp. 1158 which converted PS-5 to NS-5 (deacetylated PS-5) were separated and purified by sonication, streptomycin and ammonium sulfate fractionations, DEAE-Sephacel column chromatography and gel filtration. Molecular weight and the isoelectric point were estimated to be 75,000 and pI 5.45 for L-amino acid acylase and 100,000 and pI 4.95 for D-amino acid acylase.
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PMID:Deacetylation of PS-5, a new beta-lactam compound. II. Separation and purification of L- and D-amino acid acylases from Pseudomonas sp. 1158. 741 68

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

The basis for the difference between Campylobacter jejuni and Campylobacter coli is the presence and expression of the N-benzoylglycine amidohydrolase (hippuricase) gene only in C. jejuni. A pBR322 recombinant clone (pHIP-O) of C. jejuni TGH9011 capable of converting hippuric acid into benzoic acid and glycine, the hallmark of hippuricase activity, was characterized and sequenced. The hippuricase gene (hipO) was identified by use of deletion subclones and insertional inactivation. The transcription start point of the hippuricase gene was determined by primer extension analysis. A hippuricase-specific gene fragment was used to determine the presence of the gene in Campylobacter species. Maxicell analysis of recombinant plasmid pHIP-O by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated the production of a 42-kDa protein corresponding to the HipO gene product, in excellent agreement with the predicted molecular mass of the protein.
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PMID:Expression and characterization of Campylobacter jejuni benzoylglycine amidohydrolase (Hippuricase) gene in Escherichia coli. 773 Feb 70

A conserved amino acid sequence motif was identified in four distinct groups of enzymes that catalyze the hydrolysis of the alpha-beta phosphate bond of ATP, namely GMP synthetases, argininosuccinate synthetases, asparagine synthetases, and ATP sulfurylases. The motif is also present in Rhodobacter capsulata AdgA, Escherichia coli NtrL, and Bacillus subtilis OutB, for which no enzymatic activities are currently known. The observed pattern of amino acid residue conservation and predicted secondary structures suggest that this motif may be a modified version of the P-loop of nucleotide binding domains, and that it is likely to be involved in phosphate binding. We call it PP-motif, since it appears to be a part of a previously uncharacterized ATP pyrophophatase domain. ATP sulfurylases, NtrL, and OutB consist of this domain alone. In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain. Unexpectedly, statistically significant overall sequence similarity was found between ATP sulfurylase and 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase, another protein of the sulfate activation pathway. The PP-motif is strongly modified in PAPS reductases, but they share with ATP sulfurylases another conserved motif which might be involved in sulfate binding. We propose that PAPS reductases may have evolved from ATP sulfurylases; the evolution of the new enzymatic function appears to be accompanied by a switch of the strongest functional constraint from the PP-motif to the putative sulfate-binding motif.
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PMID:A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. 773 53

Blasticidin S (BS) deaminase (BSR) from a BS-resistant strain, Bacillus cereus K55-S1, was purified to homogeneity. Molecular weights determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and by gel filtration on HPLC are about 15500 and 35000, respectively, indicating the enzyme is a homodimer. The amino acid composition and N-terminal sequence of BSR are the same as those deduced from the nucleotide sequence of the BS-resistant gene, bsr. The optimum temperature and pH for enzyme activity are 60-65 degrees C and near 10.0, respectively. The activity of BSR is inhibited by Cu2+, Hg2+, and p-chloromercuric benzoate (PCMB). Inhibition by PCMB or HgCl2 is reversible by the addition of SH reagents. The enzyme catalyzes the deamination of BS and its derivatives, but not cytosine nucleosides.
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PMID:Inactivation of blasticidin S by Bacillus cereus. V. Purification and characterization of blasticidin S-deaminase mediated by a plasmid from blasticidin S resistant Bacillus cereus K55-S1. 774 11

Two isoforms of the heterodimeric enzyme penicillin G acylase (EC 3.5.1.11) from Providencia rettgeri ATCC 31052 (strain Bro1) were purified to near homogeneity. The isoforms exhibited comparable enzymatic activities but differed slightly in the molecular weight and pI of their respective alpha-subunit. The origin of this difference was traced to the partial conversion of the N-terminal Gln of the alpha-subunit to pyrrolidonecarboxylic acid (pyro-Glu). The boundaries of the mature enzyme within the translated DNA sequence of the wild-type propeptide (GenBank M86533) were determined. The results conclusively identified the length of the signal peptide and the position of the spacer cleaved from the propeptide to form the active heterodimer. The molecular weights of the alpha- and beta-subunits, based on these termini, were 23.7 and 62.2 kDa, respectively. Both isoforms were crystallized independently as hexagonal bipyramids up to 0.60 mm in diameter in either space group P6(1)22 or P6(5)22 (a = b = 140.5 A and c = 209.5 A) from ammonium sulfate solutions buffered by 50 mM potassium phosphate at pH 7.5. The presence of glycerol, although not required, facilitated crystal growth. Native and heavy atom derivative data were collected to 3.0 A resolution, and the calculation of isomorphous replacement phases is under way.
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PMID:Purification and preliminary crystallographic studies of penicillin G acylase from Providencia rettgeri. 779 27


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