Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The acetamidase of Mycobacterium smegmatis NCTC 8159 was purified, and the sequences of its amino-terminus and of two peptides obtained by proteolysis of the protein were obtained. A DNA fragment including the amidase structural gene was cloned in Escherichia coli, using oligonucleotide probes designed on the basis of the peptide sequences and a codon usage table calculated from published sequences of nine protein-antigen-encoding genes of the Mycobacterium tuberculosis complex. Sequence analysis of the cloned DNA revealed that the amidase gene encoded 406 amino acid residues. The nucleotide sequence close to and upstream of the amidase gene contained a probable ribosome-binding site but no identifiable promoter sequences. Three additional potential open-reading frames were found upstream of and very close to the amidase gene, with consensus '-35' and '-10' promoter sites between the first and second of these. It is hoped that the highly inducible expression of the acetamidase gene can be exploited to allow regulated expression of other genes cloned in mycobacteria.
J Gen Microbiol 1993 Mar
PMID:Cloning and sequencing of the gene which encodes the highly inducible acetamidase of Mycobacterium smegmatis. 847 63

1. The influence of strain and sex on the effect of enflurane and isoflurane and administration on heme metabolism was investigated to identify the animal model which could best reproduce the biochemical signs of acute intermittent porphyria. 2. Enflurane produced 35% and 80% increases in ALA-S activity only in CF1 male and female mice, respectively, whereas isoflurane induced 40% enzyme activity in CF1 male. 3. CF1 males showed around 35% decrease in blood PBGase and PBG-deaminase after administration of enflurane, whereas isoflurane provoked a striking inhibition (70%) in males of the C57 strain. 4. Enflurane produced alterations in heme synthesis, which would fit a model of acute porphyria in CF1 male mice. On the other hand, isoflurane would mimic biochemical alterations of this porphyria in C57 males.
Gen Pharmacol 1996 Sep
PMID:Strain and sex differences in the effect of enflurane and isoflurane on heme metabolism in mice. 890 83

1. Two new milrinone analogs, 3-acetyl-6-phenyl-2(1H)-pyridone (SF 348) and 3-acetyl-7-methyl-7,8-dihydro-2,5(1H, 6H) quinolinone (SF 349), increase the contractile activity of spontaneously beating and electrically driven atria isolated from reserpine-treated guinea-pigs. 2. Propranolol 0.1 microM drastically inhibits the contractile effect of SF 348, whereas that of SF 349 is unaffected. Preincubation of the atria with adenosine-deaminase suppresses the cardiac activity of SF 349, but does not affect that of SF 348. 3. SF 349 competitively antagonizes the negative inotropic effect induced by N6-(R-phenylisopropyl)-adenosine (R-PIA) and displaces N6-cyclohexyl[3H]-adenosine (3H-CHA) from its binding sites to A1 receptors in the guinea-pig heart. 4. The positive inotropic effect of SF 348 is largely sustained by activation of beta-adrenoceptors, whereas SF 349 acts by displacing endogenous adenosine from its inhibitory (A1) receptors in the atria.
Gen Pharmacol 1997 May
PMID:New inotropic agents: milrinone analogs. 918 20

Amiodarone (AD) is an effective antidysrythmic drug, however, there can be serious side effects, such as hepatic and neurological alterations, as well as skin photosensitization, as seen in porphyrias. Clinical signs in porphyrias might be triggered by the so-called porphyrinogenic drugs. Without sound basis, Amiodarone has been classified as an unsafe drug for porphyric patients. The aim of this work has been to study the effect of AD, both in vivo and in vitro, on heme metabolism. In the in vivo assays, the activities of 5-aminolevulinate synthetase (ALA-S), ALA dehydratase (ALA-D), porphobilinogenase (PBGase) and PBG-deaminase (PBG-D) in blood, liver, and kidney; hepatic and fecal porphyrins, urinary ALA, PBG and porphyrins in male mice strain CF1 treated with AD (100 mg i.p. daily) for 1 week and 1 month, were measured. No significanat differences were found for any of these parameters in the AD treated animals as compared to controls. In the in vitro experiments human blood, and mice blood, liver, and kidney, were used to measure the activities of ALA-S, ALA-D, PBGase, PBG-D and uroporphyrinogen decarboxylase, in the presence of varying concentrations of AD (0.0172-4.304 mM). AD did not modify any of the enzyme activities. All of the above biochemical parameters were studied in 17 cardiac patients under AD treatment for 3 to 20 years. Neither the activities of the heme enzymes, nor the levels of precursors and porphyrins in urine and plasma were altered. These findings clearly demonstrate that AD is a pharmacologically safe drug and can be used for the treatment of associated pathologies in porphyrias.
Gen Pharmacol 1999 Feb
PMID:Amiodarone is a pharmacologically safe drug for porphyrias. 1018 29

The induction of 2-amino-Delta(2)-thiazoline-4-carboxylic acid hydrolase (ATCase) and N-carbamoylcysteine amidohydrolase (NCCase), both of which are involved in the conversion step of 2-amino-Delta(2)-thiazoline carboxylic acid (ATC) to cysteine, was studied with Pseudomonas putida AJ3865. We found that L-ATC induced L-ATCase and L-NCCase, but that D-ATC induced only L-NCCase, whereas L- or D-NCC and thiazoline derivatives did not induce both enzymes. The bacterium showed neither D-ATCase nor D-NCCase activities, indicating that the role of L-ATC and D-ATC was different in the enzyme induction. We also found new inducers, d- and l-methionine, S-methyl-L-cysteine, cysteic acid, and 2-aminoethane sulfonic acid. However, the induction level of both enzymes by new inducers was much lower than those by L-ATC and D-ATC. Furthermore, the induction rate of both enzymes was synergistically increased only under a combination of D,L-ATC and new inducers. S-Compounds, however, such as new inducers except S-methyl-L-cysteine, inhibited both enzyme activities. This is the first report on the new inducers, synergistic induction, and the new inhibitors of L-ATCase and L-NCCase.
J Gen Appl Microbiol 2001 Aug
PMID:Induction of 2-amino-D2-thiazoline-4-carboxylic acid hydrolase and N-carbamoyl-l-cysteine amidohydrolase by S-compounds in Pseudomonas putida AJ3865. 1248 19

Yeast strains from the genera Candida, Debaryomyces, Aureobasidium, Geotrichum, Pichia, Rhodotorula, Tremella, Hanseniaspora, and Cryptococcus were isolated from samples of a gold mine from liquid extraction circuit. These strains were tested for their ability to utilize acetonitrile at 12 mM as the sole nitrogen source. The yeasts that grew using acetonitrile at 12 mM were tested in the presence of acetonitrile, isobutyronitrile, methacrylnitrile, and propionitrile at concentrations of 12, 24, 48, 97, and 120 mM. One strain was selected for each nitrile and the concentration of nitrile in which the best growth occurred. Cryptococcus sp. strain UFMG-Y28 had a better growth on 120 mM propionitrile and 97 mM acetonitrile, Rhodotorula glutinis strain UFMG-Y5 on 48 mM methacrylnitrile, and Cryptococcus flavus strain UFMG-Y61 on 120 mM isobutyronitrile. The utilization of different nitriles and amides by yeast strains involves hydrolysis in a two-step reaction mediated by both inducible and intracellular nitrile hydratase and amidase.
J Gen Appl Microbiol 1999 Aug
PMID:Utilization of nitriles by yeasts isolated from a Brazilian gold mine. 1250 76

The degradation of synthetic cydiastatin 4 (ARPYSFGL-amide) and cydiastatin 4 analogues cydiastatin 4alpha (PPPPPARPYSFGL-amide) and cydiastatin 4beta (PPPPPARPYSF[Acpc]L-amide) by enzymes associated with the midgut and/or haemolymph of the tobacco hawkmoth moth, Manduca sexta was investigated using reversed-phase high performance liquid chromatography (RP-HPLC) combined with matrix assisted laser desorption ionisation-time of flight mass spectrometry (MALDI-TOF MS). Cydiastatin 4 had an estimated half-life of c. 16.5min when incubated with midgut tissue in vitro and c. 2.5min with midgut lumen contents. Two degradation products were identified; cydiastatin(1-6), due to cleavage of the C-terminal di-peptide GL-amide, and cydiastatin(2-8), due to cleavage of the N-terminal A residue. Both cydiastatin 4alpha and cydiastatin 4beta had increased stability to gut and haemolymph enzymes, and full biological activity, but reduced potency compared to cydiastatin 4 when assayed on foregut peristalsis. The P-extended N-terminus of both analogues prevented hydrolysis by aminopeptidases and the replacement of the susceptible G residue with cyclopropylalanine ([Acpc]) counteracted carboxypeptidase activity. However, both analogues were susceptible to amidase-like activity giving an increase in one mass unit presumably due to the conversion of the C-terminal amide group to the free carboxylic acid. No metabolism of cydiastatin 4beta occurred when incubated with larval M. sexta haemolymph over a 90min period.
Gen Comp Endocrinol
PMID:Metabolism of cydiastatin 4 and analogues by enzymes associated with the midgut and haemolymph of Manduca sexta larvae. 1740 66

APOBEC3 cytidine deaminases hypermutate hepatitis B virus (HBV) and inhibit its replication in vitro. Whether this inhibition is due to the generation of hypermutations or to an alternative mechanism is controversial. A series of APOBEC3B (A3B) point mutants was analysed in vitro for hypermutational activity on HBV DNA and for inhibitory effects on HBV replication. Point mutations inactivating the carboxy-terminal deaminase domain abolished the hypermutational activity and reduced the inhibitory activity on HBV replication to approximately 40 %. In contrast, the point mutation H66R, inactivating the amino-terminal deaminase domain, did not affect hypermutations, but reduced the inhibition activity to 63 %, whilst the mutant C97S had no effect in either assay. Thus, only the carboxy-terminal deaminase domain of A3B catalyses cytidine deaminations leading to HBV hypermutations, but induction of hypermutations is not sufficient for full inhibition of HBV replication, for which both domains of A3B must be intact.
J Gen Virol 2007 Dec
PMID:Effects of point mutations in the cytidine deaminase domains of APOBEC3B on replication and hypermutation of hepatitis B virus in vitro. 1802 95

Ethylene inhibits the establishment of symbiosis between rhizobia and legumes. Several rhizobia species express the enzyme ACC deaminase, which degrades the ethylene precursor 1-cyclopropane-1-carboxilate (ACC), leading to reductions in the amount of ethylene evolved by the plant. M. loti has a gene encoding ACC deaminase, but this gene is under the activity of the NifA-RpoN-dependent promoter; thus, it is only expressed inside the nodule. The M. loti structural gene ACC deaminase (acdS) was integrated into the M. loti chromosome under a constitutive promoter activity. The resulting strain induced the formation of a higher number of nodules and was more competitive than the wild-type strain on Lotus japonicus and L. tenuis. These results suggest that the introduction of the ACC deaminase activity within M. loti in a constitutive way could be a novel strategy to increase nodulation competitiveness of the bacteria, which could be useful for the forage inoculants industry.
J Gen Appl Microbiol 2010 Aug
PMID:Engineered ACC deaminase-expressing free-living cells of Mesorhizobium loti show increased nodulation efficiency and competitiveness on Lotus spp. 2095 97

Elevated intracellular calcium generates rapid, profound, and irreversible changes in the nucleotide metabolism of human red blood cells (RBCs), triggered by the adenosine triphosphatase (ATPase) activity of the powerful plasma membrane calcium pump (PMCA). In the absence of glycolytic substrates, Ca(2+)-induced nucleotide changes are thought to be determined by the interaction between PMCA ATPase, adenylate kinase, and AMP-deaminase enzymes, but the extent to which this three-enzyme system can account for the Ca(2+)-induced effects has not been investigated in detail before. Such a study requires the formulation of a model incorporating the known kinetics of the three-enzyme system and a direct comparison between its predictions and precise measurements of the Ca(2+)-induced nucleotide changes, a precision not available from earlier studies. Using state-of-the-art high-performance liquid chromatography, we measured the changes in the RBC contents of ATP, ADP, AMP, and IMP during the first 35 min after ionophore-induced pump-saturating Ca(2+) loads in the absence of glycolytic substrates. Comparison between measured and model-predicted changes revealed that for good fits it was necessary to assume mean ATPase V(max) values much higher than those ever measured by PMCA-mediated Ca(2+) extrusion. These results suggest that the local nucleotide concentrations generated by ATPase activity at the inner membrane surface differed substantially from those measured in bulk cell extracts, supporting previous evidence for the existence of a submembrane microdomain with a distinct nucleotide metabolism.
J Gen Physiol 2011 Oct
PMID:Elevated intracellular Ca2+ reveals a functional membrane nucleotide pool in intact human red blood cells. 2194 47


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