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)

It is shown that potentially persistent transformation products can be formed from the herbicides bromoxynil (3,5-dibromo-4-hydroxybenzonitrile) and ioxynil (3,5-diiodo-4-hydroxybenzonitrile), and possible leaching to groundwater is discussed. A similar process to the formation of BAM (2,6-dichlorobenzamide) from the herbicide dichlobenil (2,6-dichlorobenzonitrile) can be anticipated as bromoxynil and ioxynil are analogues of dichlobenil and they are degraded by the enzymes nitrilase, nitrile hydratase and amidase. A biodegradation study using cultured Variovorax sp. DSM 11402, a species commonly found in soil, demonstrated that ioxynil and bromoxynil were fully transformed into their corresponding amides in 2-5 days. These amides were not further degraded within 18 days, and formation of other degradation products was not observed. These results are in agreement with biodegradation experiments with dichlobenil. In soil, dichlobenil is transformed into its only observed degradation product BAM, which is persistent and mobile, and has been found in 19% of 5000 samples of Danish groundwater. Variovorax sp. is known to degrade the non-halogenated analogue benzamide, suggesting that degradation of the three amides may be hindered by the halogenated substituents (meta-Br; meta-I; ortho-Cl). This hypothesis is supported by QSAR modelling of fundamental properties. Using a new optimised liquid chromatography-tandem mass spectrometry (LC-MS/MS) method, the sorption and desorption properties of bromoxynil and ioxynil were characterised in sandy topsoil at four concentration levels. The estimated sorption coefficient K(d) was 1.4 L kg(-1) for bromoxynil and 5.4 L kg(-1) for ioxynil, indicating weak to moderate sorption to topsoil. Desorption of the herbicides showed that they were strongly and irreversible bound to the soil (K(des) > K(d)). The amount of herbicide desorbed depended on the initial concentration level. At low levels, K(des) values were higher, indicating stronger binding than at higher levels. The isocratic LC-MS/MS method developed for simultaneous detection of bromoxynil, ioxynil and their main degradation products is described. Using negative electrospray ionisation (ESI-), the detection limits were 0.4-1.0 microg L(-1), with relative standard deviations of 4-10% (n = 10) using direct injection without clean-up steps. The standard curves showed linearity in the range 5-100 microg L(-1) with r(2) > 0.992.
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PMID:Demonstrating formation of potentially persistent transformation products from the herbicides bromoxynil and ioxynil using liquid chromatography-tandem mass spectrometry (LC-MS/MS). 1712 53

The tandem conversion process involving nitrile hydratase- and amidase-producing microorganisms has potential for use in the treatment of acetonitrile-containing wastes. In that process, the acetamide hydrolysis step catalyzed by amidase is very slow compared with the acetonitrile hydration step catalyzed by nitrile hydratase, and a small amount of acetamide remains in the resulting solution. This study aimed to improve the efficiency of the acetamide hydrolysis step. An amidase-producing microorganism, Rhodococcus sp. S13-4, was newly obtained, whose use enabled rapid acetamide degradation. Though residual acetamide was still detected, it was successfully reduced by the addition of cation/anion mixed ion exchange resin or calcium hydroxide after the acetamide hydrolysis reaction using Rhodococcus sp. S13-4 cells. This result implies that acetamide hydrolysis and acetamide formation are in equilibrium. The incubation of Rhodococcus sp. S13-4 cells with high concentrations of ammonium acetate produced acetamide. The purified amidase from Rhodococcus sp. S13-4 revealed the acetamide formation activity (specific activity of 30.6 U/mg protein). This suggests that the amidase-catalyzed amide formation may cause the remaining of acetamide in the acetonitrile conversion process.
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PMID:Remaining acetamide in acetonitrile degradation using nitrile hydratase- and amidase-producing microorganisms. 1713 68

Biotransformations of 3-arylpent-4-enenitriles catalyzed by Rhodococcus erythropolis AJ270, a nitrile hydratase/amidase-containing microbial whole-cell catalyst were studied, and an unusual beta-vinyl effect of the substrate on the biocatalytic efficiency and enantioselectivity of the amidase was observed. While 3-arylpent-4-enenitriles and 3-phenylpentanenitrile were efficiently hydrated by the action of the less R-enantioselective nitrile hydratase, the amidase showed greater activity and higher enantioselectivity against 3-arylpent-4-enoic acid amides than 3-arylpentanoic acid amides. Under very mild conditions, nitrile biotransformations provided an efficient synthesis of highly enantiopure (R)-3-arylpent-4-enoic acids and (S)-3-arylpent-4-enoic acid amides, and their applications were demonstrated by the synthesis of chiral gamma-amino acid, 2-pyrrolidinone, and 2-azepinone derivatives.
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PMID:An unusual beta-vinyl effect leading to high efficiency and enantioselectivity of the amidase, nitrile biotransformations for the preparation of enantiopure 3-arylpent-4-enoic acids and amides and their applications in synthesis. 1713 91

Catalyzed by the Rhodococcus erythropolis AJ270 whole cell catalyst under very mild conditions, biotransformations of racemic 1-arylaziridine-2-carbonitriles proceeded efficiently and enantioselectively to produce highly enantiopure S-1-arylaziridine-2-carboxamides and R-1-arylaziridine-2-carboxylic acids in excellent yields. Although the nitrile hydratase exhibits no selectivity against all nitrile substrates, the amidase is highly R-enantioselective towards 1-arylaziridine-2-carboxamides. When treated with benzyl bromide, 1-phenylaziridine-2S-carboxamide underwent a highly regioselective and enantiospecific ring-opening reaction to afford an almost quantitative yield of R-beta-[(benzyl)phenylamino]-alpha-bromopropanamide (C-2 attack) and R-alpha-[(benzyl)phenylamino]-beta-bromopropanamide (C-3 attack) in a 10.5:1 ratio. Further treatment of the resulting ring-opening products with an N-nucleophilic reagent such as amine and azide led to, through most probably the aziridinium intermediate, the formation of S-alpha-substituted-beta-[(benzyl)phenylamino]propanamides in good chemical yields with high enantiomeric purity.
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PMID:Nitrile biotransformations for the efficient synthesis of highly enantiopure 1-arylaziridine-2-carboxylic acid derivatives and their stereoselective ring-opening reactions. 1728 38

Nitriles are important environmental compounds, both as natural products and industrial pollutants. Until now, there have been no data on the possibility of microbial nitrile degradation at high pH/salt conditions. Acetonitrile (CH(3)C(triple bond)N) is the simplest organic nitrile. Here, evidence is provided of microbial utilization of acetonitrile as a carbon, energy and nitrogen source at extremely high pH and moderate salinity. Positive enrichment cultures with acetonitrile at pH 10 and salt content equivalent to 0.6 M total Na(+) were obtained from mixed sediment samples from soda lakes, but not from soda soils. Purification of these cultures resulted in the isolation of two bacterial strains capable of growth with acetonitrile as sole carbon, energy and nitrogen source under haloalkaline conditions. Apart from acetonitrile, the bacteria also grew with propionitrile. Nitrile hydrolysis to acetamide was identified as the rate-limiting step of acetonitrile degradation via the nitrile hydratase/amidase pathway. The new bacteria belonged to moderately salt-tolerant obligate alkaliphiles with optimum growth at pH 10 and 0.5 M total Na(+). The cells were yellow-coloured due to a high concentration of carotenoids dominated by zeaxanthin. Phylogenetic analysis placed the isolates into a new lineage within the family Ectothiorhodospiraceae in the Gammaproteobacteria. On the basis of unique phenotypic properties and their separate phylogenetic position, the new bacteria are placed into a new genus and species for which the name Natronocella acetinitrilica gen. nov., sp. nov is proposed.
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PMID:Acetonitrile degradation under haloalkaline conditions by Natronocella acetinitrilica gen. nov., sp. nov. 1737 25

A microbial process for the degradation of three types of structurally distinct organonitriles (i.e., saturated and unsaturated aliphatic nitrile and aromatic nitrile) was studied. Microorganisms were enriched from the activated sludge of a pharmaceutical wastewater treatment plant and adapted through providing acetonitrile as the sole carbon and nitrogen source for their growth. The adapted mixed culture was then examined for their capability of degrading acetonitrile, acrylonitrile and benzonitrile under various operational conditions. The performance of biodegradation and the metabolic intermediate- and end-products in the process were monitored. The results show that an average removal rate of 0.083 g acetonitrile g(-1)-VSS h(-1), 0.0074 g acrylonitrile g(-1)-VSS h(-1) or 0.0029 g benzonitrile g(-1)-VSS h(-1) was achieved in the batch bioreactor under the common operational condition of 25 degrees C and pH 7. The biodegradation of acetonitrile and acrylonitrile showed a two-step pathway, with the generation of acetamide followed by acetic acid and ammonia for acetonitrile or acrylamide followed by acrylic acid and ammonia for acrylonitrile. However, the biodegradation of benzonitrile appeared to have only one step, with the direct production of benzoic acid and ammonia, but without benzamide being detected in the process. The results suggest that, depending on the substrates, the adapted mixed culture can develop very different degradation pathways, such as nitrile hydratase plus amidase for acetonitrile or acrylonitrile and nitrilase for benzonitrile. Therefore, the adapted mixed culture has a great potential and flexibility for actual applications in biodegradation of various organonitrile compounds.
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PMID:Biodegradation of organonitriles by adapted activated sludge consortium with acetonitrile-degrading microorganisms. 1754 72

A mutant of the cysteine protease papain, displaying nitrile hydratase and amidase activities, was expressed in Pichia pastoris and used for the hydrolysis of peptide nitriles in aqueous-organic media. The rate of hydrolysis of these nitriles is lowered by increasing acetone concentration. This is caused by an increase of the Michaelis constant, and a variation of Vmax proportional to the amount of water in the mixture. The hydrolysis of the amide is less affected by the increase in co-solvent, which results in lower accumulation of this intermediate product. With the peptide nitrile tested, high nitrile concentrations could be used to promote the production of the amide and prevent its hydrolysis to the acid by diminishing the relative rate of amide hydrolysis. A number of non-peptidyl nitriles were also tested as potential substrates but activity was detected for only one compound with structural resemblance to peptide nitriles.
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PMID:Enzymatic hydrolysis of nitriles by an engineered nitrile hydratase (papain Gln19Glu) in aqueous-organic media. 1759 Sep 26

Biotransformations of various functionalized racemic nitriles catalyzed by Rhodococcus erythropolis AJ270, a nitrile hydratase/amidase-containing microbial whole-cell catalyst, were studied. While the nitrile hydratase exhibits high catalytic efficiency but very low enantioselectivity against almost all nitrile substrates examined, the amidase is very sensitive toward the structure of the amides. The release of the steric crowdedness around the stereocenter of the substrates and the introduction of an unsaturated carbon-carbon bond into the substrates led to the significant acceleration of the reaction rate and the dramatic enhancement of the enantioselectivity. Nitrile biotransformations provide a unique and high-yielding synthetic route to highly enantiopure carboxylic acids and amides functionalized with an allyl, propargyl, allenyl, or vinyl group. The synthetic applications have been demonstrated by the synthesis of enantiopure heterocyclic compounds including iodoenol gamma-lactone, gamma-lactam, and 3-allyl-1-phenyl-3,4-dihydro-1H-quinolin-2-one derivatives.
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PMID:Remarkable electronic and steric effects in the nitrile biotransformations for the preparation of enantiopure functionalized carboxylic acids and amides: implication for an unsaturated carbon-carbon bond binding domain of the amidase. 1760 98

The microbial degradation of nitriles is of interest for bioremediation and green chemistry. We demonstrated that the soil bacterium Rhodococcus sp. RHA1 utilizes a range of nitriles, including acetonitrile, as growth substrates. Proteomic analysis identified 13 proteins that were more abundant in acetonitrile-grown cells, including an aliphatic amidase and a protein with no known homologue. Purification of a nitrile hydratase (NHase) from acetonitrile-grown cells identified the unknown protein as the beta subunit of a two-subunit NHase. Sequence analysis revealed that the genes encoding the amidase (anhC) and the NHase (anhAB) occur in a 12.8 kbp cluster located on plasmid pRHL2. The anh gene cluster also encodes an acetyl-CoA hydrolase, transcriptional regulators, a putative cobalt transporter and a protein of unknown function. Striking features of the NHase include the amino acid sequence identity (32%) and large size (63 and 56 kDa) of the alpha and beta subunits, as well as the enzyme's metal ion content (one cobalt, two copper and one zinc). The enzyme possessed similar specificities for acetonitrile and propionitrile (k(cat)/K(m) approximately 7 mM(-1) s(-1)) followed by acrylonitrile and butyronitrile. We propose that this acetonitrile hydratase (ANHase) represents the first member of a previously unknown class of NHases.
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PMID:Purification and characterization of a novel nitrile hydratase from Rhodococcus sp. RHA1. 1763 93

The utilization of isobutyronitrile (iBN) as a C and N source under haloalkaline conditions by microbial communities from soda lake sediments and soda soils was studied. In both cases, a consortium consisting of two different bacterial species capable of the complete degradation and utilization of iBN at pH 10 was selected. The soda lake sediment consortium consisted of a new actinobacterium and a gammaproteobacterium from the genus Marinospirillum. The former was capable of fast hydrolysis of aliphatic nitriles to the corresponding amides and much-slower further hydrolysis of the amides to carboxylic acids. Its partner cannot hydrolyze nitriles but grew rapidly on amides and carboxylic acids, thus acting as a scavenger of products released by the actinobacterium. The soda soil consortium consisted of two Bacillus species (RNA group 1). One of them initiated nitrile hydrolysis, and the other utilized the hydrolysis products isobutyroamide (iBA) and isobutyrate (iB). In contrast to the actinobacterium, the nitrile-hydrolyzing soil Bacillus grew rapidly with hydrolysis products, but it was dependent on vitamins most probably supplied by its product-utilizing partner. All four bacterial strains isolated were moderately salt-tolerant alkaliphiles with a pH range for growth from pH 7.0 to 8.5 up to 10.3 to 10.5. However, both their nitrile hydratase and amidase activities had a near-neutral pH optimum, indicating an intracellular localization of these enzymes. Despite this fact, the study demonstrated a possibility of whole-cell biocatalytic hydrolysis of various nitriles at haloalkaline conditions.
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PMID:Microbial isobutyronitrile utilization under haloalkaline conditions. 1764 41


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