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 amidase genes of Pseudomonas aeruginosa were inserted into a lambda replacement vector following cleavage with the restriction endonuclease HindIII. The recombinant lambdaami was detected by enhanced growth of Escherichia coli around plaques of the recombinant phage on minimal medium containing acetamide as the nitrogen source. Low levels of amidase activity were detected in E. coli cultures infected with lambdaami and these were sufficient to allow growth with acetamide as nitrogen source. Lysis-defective derivatives of lambdaami were made by introducing Q-, S-, mutations. Cultures of E. coli infected with lambdaamiQ-S- synthesised amidase as the major protein. The amidase produced by these cultures was identical to that produced by PAC strains of P. aeruginosa in substrate specificty, thermal stability and immunological cross-reaction.
Mol Gen Genet 1980 Jan
PMID:The construction in vitro of derivatives of bacteriophage lambda carrying the amidase genes of Pseudomonas aeruginosa. 624 42

As reported by Jamieson and Subak-Sharpe (J. Gen. Virol. 31:303-313, 1976), exogenous deoxycytidine is very poorly incorporated into herpes simplex virus DNA. Here it is shown that this incorporation was dramatically increased in the presence of tetrahydrouridine (THU), a specific inhibitor of cytidine-deoxycytidine deaminase. Thus, the exclusion of deoxycytidine from herpes simplex virus DNA probably results from massive degradation by the deaminase, which is consistent with the observation that in the absence of THU, most of the nucleotides formed from exogenous deoxycytidine are dUMP. The effect of tHU upon deoxycytidine incorporation was specific for herpes simplex virus-infected cells; THU did not increase deoxycytidine incorporation into DNA of uninfected cells. Therefore, one might expect THU to enhance the antiviral activity of 1-beta-D-arabinofuranasylcytosine since this analog is also readily deaminated. However, THU increased both the antiviral activity and the cell toxicity only slightly and to about the same extent. Therefore, the metabolism of 1-beta-D-arabnofuranosylcytosine is different from that of deoxycytidine in herpes simplex virus-infected cells.
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PMID:Tetrahydrouridine specifically facilitates deoxycytidine incorporation into herpes simplex virus DNA. 626 39

Deoxycytidine (dC) deaminase activity has been previously reported to be induced in herpes simplex virus (HSV)-infected cells (Chan, 1977). In contrast, we report here that HSV infection of either hamster cells naturally deficient in this enzyme activity or mouse cells containing a low level of activity never resulted in appearance of stimulation of dC deaminase, whereas thymidine kinase (TK) was always induced. Surprisingly, dC deaminase activity, which differed by electrophoretic mobility from the mouse or human cell enzyme, was discovered in some cells selected for the presence of HSV TK after infection with u.v.-irradiated HSV. Evidence is presented which suggests that the appearance of this new enzyme was not due to the presence of virus genes but rather to mycoplasma contamination.
J Gen Virol 1981 Nov
PMID:Analysis of deoxycytidine (dC) deaminase activity in herpes simplex virus-infected or HSV TK-transformed cells: association with mycoplasma contamination but not with virus infection. 627 19

The enzymes of N-acetyl-D-glucosamine (GlcNAc) metabolism, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase were found to be inducible in Candida albicans. The pattern of induction for these enzymes was the same under conditions of germ-tube formation (37 degrees C) and where yeast cells metabolized GlcNAc with no change in morphology (28 degrees C); this indicates that these enzymes are not control points in the dimorphic development of C. albicans. During induction there was a 40-and 25-fold increase in specific activity for the deacetylase and the deaminase, respectively, and the maximum specific activity correspond to the time when all the GlcNAc had been metabolized. The presence of lomofungin (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans containing GlcNAc prevented the increase in specific activity of these enzymes. 2-Deoxyglucose inhibited germ-tube formation, partially inhibited the induction of the deacetylase (43%) and the deaminase (60%), but did not affect the growth of C. albicans on either Glc or GlcNAc. GlcN-6-phosphate was a competitive inhibitor of the deacetylase with a Ki of 1.4 mM while the other product of the reaction, acetate, did not inhibit the enzyme. The Km value for GlcN-6-phosphate on GlcN-6-phosphate deaminase was 0.24 mM. Incubation of starved yeast cells with GlcNAc produced a four-fold increase in the specific activity of UDP-GlcNAc-pyrophosphorylase at either 28 degrees C or 37 degrees C.
J Gen Microbiol 1982 Oct
PMID:Enzymes of N-acetylglucosamine metabolism during germ-tube formation in Candida albicans. 629 72

A plasmid, pCL34, capable of autonomous replication in Escherichia coli and Pseudomonas aeruginosa has been constructed which carries the promoter and structural gene (amiE) for P. aeruginosa amidase, but not the regulator gene (amiR). Plasmid pCL34 has been mobilized from E. coli to P. aeruginosa using the broad host range plasmid RP4. Complementation studies were performed in P. aeruginosa strains carrying various amidase mutations. Measurements of amidase activity in the recipients under inducing, non-inducing and repressing conditions showed trans-complementation by the chromosomally located regulator gene product. These results confirmed the positive control model for amidase gene expression. Levels of amidase expression seen during these studies were approximately threefold higher than in the parental, amidase-positive strains.
J Gen Microbiol 1984 Dec
PMID:Complementation analysis of the aliphatic amidase genes of Pseudomonas aeruginosa. 644 Sep 48

1. The effect of enflurane or isoflurane anesthesia (1 ml/kg, i.p.) in animals chronically treated with ethanol (30%, v/v, in drinking water during a week) on heme metabolism and its regulation was investigated. 2. In those animals previously intoxicated with ethanol that received isoflurane, ALA-S activity was increased (control values: 0.071 +/- 0.022 nmol/mg, n = 10; treated animals: 0.110 +/- 0.034 nmol/mg, n = 8) and blood PBGase and deaminase were strikingly diminished (control values, n = 10: PBGase: 0.101 +/- 0.015 nmol/mg, deaminase: 0.242 +/- 0.075 nmol/mg; treated animals, n = 6: PBGase: 0.063 +/- 0.013 nmol/mg; deaminase: 0.145 +/- 0.045 nmol/mg). 3. The time-response study showed that liver ALA-S is enhanced at shorter times of anesthesia with isoflurane and that blood PBGase and deaminase appeared inhibited later in animals previously treated with ethanol. 4. Results reproduce some biochemical alterations known to occur in acute intermittent porphyria.
Gen Pharmacol 1995 Oct
PMID:Alterations in fluorinated ether anesthetics effects on heme metabolism following chronic ethanol consumption. 759 Jan 42

1. The effect of the administration of several doses of Enflurane and Isoflurane (2 ml/kg, i.p., daily) on heme metabolism and glucose levels was studied. 2. Liver and kidney delta-Aminolevulinic acid synthetase (ALA-S) activities were 85% (P < 0.01) induced after the third dose of Enflurane, instead induction of this enzyme was only detected, in animals receiving one dose of Isoflurane. 3. Blood Porphobilinogenase and deaminase (50%, P < 0.01) inhibition was produced only when animals received a single dose of the anesthetics. 5. ALA-S induction observed after the third dose of anesthetics could be a consequence of long lasting depletion in heme synthesis produced by blocking at uroporphyrinogen level.
Gen Pharmacol 1994 Oct
PMID:Effect of multiple doses of volatile anesthetics on heme enzymes. 787 42

We have cloned a DNA fragment containing the gene for a cell wall hydrolase from Bacillus licheniformis FD0120 into Escherichia coli. Sequencing of the fragment showed the presence of an open reading frame (ORF; designated as cwlL), which is different from the B. licheniformis cell wall hydrolase gene cwlM, and encodes a polypeptide of 360 amino acids with a molecular mass of 38,994. The enzyme purified from the E. coli clone is an N-acetylmuramoyl-L-alanine amidase, which has a M(r) value of 41 kDa as determined by SDS-polyacrylamide gel electrophoresis, and is able to digest B. licheniformis, B. subtilis and Micrococcus luteus cell walls. The nucleotide and deduced amino acid sequences of cwlL are very similar to those of ORF3 in the putative operon xpaL1-xpaL2-ORF3 in B. licheniformis MC14. Moreover, the amino acid sequence homology of CwlL with the B. subtilis amidase CwlA indicates two evolutionarily distinguishable regions in CwlL. The sequence homology of CwlL with other cell wall hydrolases and the regulation of cwlL are discussed.
Mol Gen Genet 1993 Nov
PMID:Molecular cloning, sequence analysis, and characterization of a new cell wall hydrolase, CwlL, of Bacillus licheniformis. 790 27

The CWLA lytic amidase of Bacillus subtilis 168 was purified and antisera raised against the purified protein. No expression of cwlA could be demonstrated under any conditions by the use of the antisera and cwlA::lacZ fusion analysis. Two lytic enzymes of apparent molecular masses 34 and 30 kDa (as measured by renaturing SDS-PAGE) were found to be mitomycin C-inducible, the larger of which corresponds to a protein immunologically related to CWLA. Both of these inducible lysins were found to be encoded by prophage PBSX. Prophage SP beta was shown by renaturing SDS-PAGE to produce a 43 kDa lytic enzyme unrelated immunologically to CWLA. The smaller of the two PBSX enzymes was purified and found to be an N-acetylmuramyl-L-alanine amidase of 32 kDa (as measured by SDS-PAGE and Coomassie blue staining) which cross-reacts only weakly with the anti-CWLA sera. The potential origin of cwlA and its possible relationship to the other phage lytic enzymes are discussed.
J Gen Microbiol 1993 Dec
PMID:Analysis of Bacillus subtilis 168 prophage-associated lytic enzymes; identification and characterization of CWLA-related prophage proteins. 790 56

Aspergillus terreus produces a unique enzyme, blasticidin S deaminase, which catalyzes the deamination of blasticidin S (BS), and in consequence confers high resistance to the antibiotic. A cDNA clone derived from the structural gene for BS deaminase (BSD) was isolated by transforming Escherichia coli with an Aspergillus cDNA expression library and directly selecting for the ability to grow in the presence of the antibiotic. The complete nucleotide sequence of BSD was determined and proved to contain an open reading frame of 393 bp, encoding a polypeptide of 130 amino acids. Comparison of its nucleotide sequence with that of bsr, the BS deaminase gene isolated from Bacillus cereus, indicated no homology and a large difference in codon usage. The activity of BSD expressed in E. coli was easily quantified by an assay based on spectrophotometric recording. The BSD gene was placed in a shuttle vector for Schizosaccharomyces pombe, downstream of the SV40 early region promoter, and this allowed direct selection with BS at high frequency, following transformation into the yeast. The BSD gene was also employed as a selectable marker for Pyricularia oryzae, which could not be transformed to BS resistance by bsr. These result promise that the BSD gene will be useful as a new dominant selectable marker for eukaryotes.
Mol Gen Genet 1994 Jan
PMID:Cloning of the blasticidin S deaminase gene (BSD) from Aspergillus terreus and its use as a selectable marker for Schizosaccharomyces pombe and Pyricularia oryzae. 815 61


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