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)

A gram-negative rod-shaped bacterium capable of utilizing acrylonitrile as the sole source of nitrogen was isolated from industrial sewage and identified as Klebsiella pneumoniae. The isolate was capable of utilizing aliphatic nitriles containing 1 to 5 carbon atoms or benzonitrile as the sole source of nitrogen and either acetamide or propionamide as the sole source of both carbon and nitrogen. Gas chromatographic and mass spectral analyses of culture filtrates indicated that K. pneumoniae was capable of hydrolyzing 6.15 mmol of acrylonitrile to 5.15 mmol of acrylamide within 24 h. The acrylamide was hydrolyzed to 1.0 mmol of acrylic acid within 72 h. Another metabolite of acrylonitrile metabolism was ammonia, which reached a maximum concentration of 3.69 mM within 48 h. Nitrile hydratase and amidase, the two hydrolytic enzymes responsible for the sequential metabolism of nitrile compounds, were induced by acrylonitrile. The optimum temperature for nitrile hydratase activity was 55 degrees C and that for amidase was 40 degrees C; both enzymes had pH optima of 8.0.
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PMID:Metabolism of acrylonitrile by Klebsiella pneumoniae. 195 6

A variant of a yeast strain identified as Candida famata isolated from gold mine effluent was able to grow on acetonitrile, acrylonitrile, butyronitrile, isobutyronitrile, methacrylnitrile, propionitrile, succinonitrile, valeronitrile, acetamide, isobutyamide, and succinamide as sole nitrogen source, after acclimatization. The yeast grew on acetonitrile and acetamide at concentrations up to 4%. The utilisation of acetonitrile and acetamide by the C. famata strain probably involves hydrolysis in a two-step reaction mediated by both inducible and intracellular nitrile hydratase and amidase.
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PMID:Utilization of acetonitrile and other aliphatic nitriles by a Candida famata strain. 887 Feb 54

Rhodococci are ubiquitous in nature and their ability to metabolise a wide range of chemicals, many of which are toxic, has given rise to an increasing number of studies into their diverse use as biocatalysts. Indeed rhodococci have been shown to be especially good at degrading aromatic and aliphatic nitriles and amides and thus they are very useful for waste clean up where these toxic chemicals are present. The use of biocatalysts in the chemical industry has in the main been for the manufacture of high-value fine chemicals, such as pharmaceutical intermediates, though investigations into the use of nitrile hydratase, amidase and nitrilase to convert acrylonitrile into the higher value products acrylamide and acrylic acid have been carried out for a number of years. Acrylamide and acrylic acid are manufactured by chemical processes in vast tonnages annually and they are used to produce polymers for applications such as superabsorbents, dispersants and flocculants. Rhodococci are chosen for use as biocatalysts on an industrial scale for the production of acrylamide and acrylic acid due to their ease of growth to high biomass yields, high specific enzyme activities obtainable, their EFB class 1 status and robustness of the whole cells within chemical reaction systems. Several isolates belonging to the genus Rhodococcus have been shown in our studies to be among the best candidates for acrylic acid preparation from acrylonitrile due to their stability and tolerance to high concentrations of this reactive and disruptive substrate. A critical part of the selection procedure for the best candidates during the screening programme was high purity product with very low residual substrate concentrations, even in the presence of high product concentrations. Additionally the nitrile and amide substrate scavenging ability which enables rhodococci to survive very successfully in the environment leads to the formation of biocatalysts which are suitable for the removal of low concentrations of acrylonitrile and acrylamide in waste streams and for the removal of impurities in manufacturing processes.
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PMID:Application of whole cell rhodococcal biocatalysts in acrylic polymer manufacture. 1006 94

A thermophilic Bacillus spp. capable of transforming aliphatic nitriles, cyclic nitriles and dinitriles was used as a free cell suspension and immobilized in alginate beads to study the utilization of acetonitrile and acrylonitrile in a buffered biotransformation medium. The cells grew optimally at 65 degrees C and contained a nitrile hydratase-amidase enzyme system that transformed nitrile compounds stoichiometrically to the corresponding carboxylic acids. In the presence of urea or chloroacetone, amidase activity was inhibited and the amide intermediate was accumulated. Mass transfer limitation of nitrile utilization rates was observed with immobilized cells, but the alginate afforded the cells some degree of additional thermal stability and potential advantage in re-use. In vitro inhibition of the partially purified amidase was confirmed and the use of whole cells of this organism in a continuous bioreactor to generate amide products from nitrile substrates was demonstrated.
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PMID:Nitrile biotransformations using free and immobilized cells of a thermophilic Bacillus spp. 1071 9

A moderate thermophile, Bacillus sp. BR449 was previously shown to exhibit a high level of nitrile hydratase (NHase) activity when growing on high levels of acrylonitrile at 55 degrees C. In this report, we describe the cloning of a 6.1 kb SalI DNA fragment encoding the NHase gene cluster of BR449 into Escherichia coli. Nucleotide sequencing revealed six ORFs encoding (in order), two unidentified putative proteins, amidase, NHase beta- and alpha-subunits and a small putative protein of 101 amino acids designated P12K. Spacings and orientation of the coding regions as well as their gene expression in E. coli suggest that the beta-subunit, alpha-subunit, and P12K genes are co-transcribed. Analysis of deduced amino acid sequences indicate that the amidase (348 aa, MW 38.6 kDa) belongs to the nitrilase-related aliphatic amidase family, and that the NHase beta- (229 aa, MW 26.5 kDa) and alpha- (214 aa, MW 24.5 kDa) subunits comprise a cobalt-containing member of the NHase family, which includes Rhodococcus rhodochrous J1 and Pseudomonas putida 5B NHases. The amidase/NHase gene cluster differs both in arrangement and composition from those described for other NHase-producing strains. When expressed in Escherichia coli DH5alpha, the subcloned NHase genes produced significant levels of active NHase enzyme when cobalt ion was added either to the culture medium or cell extracts. Presence of the P12K gene and addition of amide compounds as inducers were not required for this expression.
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PMID:Cloning and expression of the nitrile hydratase and amidase genes from Bacillus sp. BR449 into Escherichia coli. 1097 71

The respiratory activity of Rhodococcus rhodochrous M8 cells containing nitrile hydratase and amidase was studied in the presence of nitriles and amides of carbonic acids. Culturing of cells with acrylonitrile and acrylamide yielding their maximum respiratory activity was studied. The optimum conditions for measurements and maintenance of respiratory activity were found. Curves for the linear concentration dependence of cell respiratory activity on 0.01-0.5 mM acrylonitrile, 0.025-1.0 mM acetonitrile, and 0.01-0.1 mM acrylamide were plotted. The selectivity of cell respiratory activity for some substrates was analyzed.
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PMID:[The respiratory activity of Rhodococcus rhodochrous M8 cells producing nitrile-hydrolyzing enzymes]. 1144 2

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

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

Acrylamide was produced from acrylonitrile using immobilized Brevibacterium CH1 cells that were isolated from soil and found to possess nitrile hydratase activity. The reaction conditions and stability of the enzyme activity were studied. The conversion yield was nearly 100%, including a trace amount of acrylic acid. This strain showed strong activity of nitrile hydratase toward acrylonitrile and extremely low activity of amidase toward acrylamide. A packed bed reactor was operated in a fed-batch manner for acrylamide production of high concentration. The acrylonitrile concentration was maintained below 3% and the operating temperature at 4 degrees C to minimize enzyme deactivation.
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PMID:Biotransformation of acrylonitrile to acrylamide using immobilized whole cells of Brevibacterium CH1 in a recycle fed-batch reactor. 1858 14

An enrichment culture from saline soda soils, using acetate as carbon and energy source and 2-phenylpropionitrile as nitrogen source (PPN) at pH 10, resulted in the isolation of strain ANL-alpha CH3. The strain was identified as a representative of the genus Halomonas in the Gammaproteobacteria. The bacterium was capable of PPN utilization as a nitrogen source only, while phenylacetonitrile (PAN) served both as carbon, energy and nitrogen source. This capacity was not described previously for any other haloalkaliphilic bacteria. Apart from the nitriles mentioned above, resting cells of ANL-alpha CH3 also hydrolyzed mandelonitrile, benzonitrile, acrylonitrile, and phenylglycinonitrile, presumably using nitrilase pathway. Neither nitrile hydratase nor amidase activity was detected. The isolate showed a capacity to grow with benzoate and salicylate as carbon and energy source and demonstrated the ability to completely mineralize PAN. These clearly indicated a potential to catabolize aromatic compounds. On the basis of unique phenotype and distinct phylogeny, strain ANL-alpha CH3 is proposed as a novel species of the genus Halomonas--Halomonas nitrilicus sp. nov.
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PMID:Utilization of arylaliphatic nitriles by haloalkaliphilic Halomonas nitrilicus sp. nov. isolated from soda soils. 1879 82


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