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Showing 1 to 12 of 12 for “"Nitrilase"”.

  1. The structure of the nitrilase from Rhodococcus Rhodochrous J1: homology modeling and three-dimensional reconstruction

    The nitrilases are an important class of industrial enzymes that are found in all phyla. These enzymes are expressed widely in prokaryotes and eukaryotes. Nitrilases convert nitriles to corresponding acids and ammonia. They are used in industry as biocatalysts because of their specificity and …

    western-cape Repository record for The structure of the nitrilase from Rhodococcus Rhodochrous J1: homology modeling and three-dimensional reconstruction (opens in a new tab)

  2. Nitrilase 2: insight into its regulation in Arabidopsis and its potential for improving maize salt tolerance

    … auxin levels increase under saline conditions. Nitrilase 2 was identified as the biosynthetic gene possibly responsible for these changes in auxin accumulation as AtNit2 expression was elevated specifically under saline conditions. Additionally, AtNit2 overexpression lines were more salt …

    cape-town Repository record for Nitrilase 2: insight into its regulation in Arabidopsis and its potential for improving maize salt tolerance (opens in a new tab)

  3. The crystal structure of an aliphatic amidase from Geobacillus pallidus RAPc8

    … RAPcS (RAPcS amidase), which belongs to the nitrilase superfamily of enzymes, has recently been characterised biochemically. It shows both amide hydrolysis and acyl transfer activities, and also exhibits stereo selectivity for some enantiomeric substrates. This enzyme can therefore be …

    cape-town Repository record for The crystal structure of an aliphatic amidase from Geobacillus pallidus RAPc8 (opens in a new tab)

  4. Engineering cyanide-tolerant Arabidopsis thaliana

    … asparagine, or aspartate and ammonia, by plant nitrilase 4 enzymes. β-Cyanoalanine synthase activity enables plants to detoxify limited concentrations of exogenous cyanide. However, phytotoxicity and death occur from exposure to relatively low concentrations of exogenous cyanide. In contrast, …

    cape-town Repository record for Engineering cyanide-tolerant Arabidopsis thaliana (opens in a new tab)

  5. Factors involved in the oligomerisation of the cyanide dihydratase from Bacillus pumilus C1

    … Bacillus pumilus C1 (CynDₚᵤₘ) is a member of the nitrilase superfamily and is known to specifically catalyse the conversion of cyanide into formic acid and ammonia. This enzyme is a good candidate for bioremediation of cyanide waste but the high alkaline pH of the cyanide waste water poses a …

    cape-town Repository record for Factors involved in the oligomerisation of the cyanide dihydratase from Bacillus pumilus C1 (opens in a new tab)

  6. Isolation, identification and characterisation of novel actinobacteria from Zambian hot-springs

    … has hydantoinase, carbamoylase, amidase and nitrilase activities.The Streptomyces sp. hydantionase was cloned and functionally expressed in E.coli. The recombinant enzyme showed 49 % similarity to a crystallised hydantoinase from a Bacillus species. Homology modelling revealed that the enzyme …

    western-cape Repository record for Isolation, identification and characterisation of novel actinobacteria from Zambian hot-springs (opens in a new tab)

  7. Activity of the beta-cyanoalanine synthase pathway is associated with the response to abiotic stress by Arabidopsis thaliana.

    … synthase and cysteine synthase. A dual nitrilase 4 enzyme then converts the β-cyanoalanine into asparagine or aspartate and ammonium. Studies have suggested that the physiological function of the pathway is not restricted to detoxification and assimilation of excess cyanide. The overall …

    siu-theses Repository record for Activity of the beta-cyanoalanine synthase pathway is associated with the response to abiotic stress by Arabidopsis thaliana. (opens in a new tab)

  8. Ph-dependence of the quaternary structure of the cyanide dihydratase from bacillus pumilus

    Nitrilases are moderately ubiquitous nitrile/cyanide-degrading enzymes, found in both eukaryotes (animals, fungi, plants) and prokaryotes (archaea, bacteria) which catalyse the condensation and hydrolysis of a wide range of non-peptide nitrile substrates and are involved in …

    cape-town Repository record for Ph-dependence of the quaternary structure of the cyanide dihydratase from bacillus pumilus (opens in a new tab)

  9. Analysis and Redesign of Protein-Protein Interactions: A Hotspot-Centric View

    … and is conserved between many homologues in the nitrilase superfamily, meeting one of the key criteria by which potential hotspots can be identified. This analysis supports a number of analogies between hotspot residues and catalytic residues in enzyme active sites, and raises the intriguing …

    duke Repository record for Analysis and Redesign of Protein-Protein Interactions: A Hotspot-Centric View (opens in a new tab)

  10. Characterisation of auxin and auxin-related genes in the response of Arabidopsis thaliana to salt stress

    … observed for IAA. Additionally, mRNA levels of Nitrilase 2 (which converts IAN to IAA) were significantly increased in response to NaCl but not sorbitol. Taken together, these results suggest that IAA biosynthesis is increased in response to NaCl via the hydrolysis of IAN to IAA by NIT2. In …

    cape-town Repository record for Characterisation of auxin and auxin-related genes in the response of Arabidopsis thaliana to salt stress (opens in a new tab)

  11. Investigating the molecular mechanism whereby auxin modulates Arabidopsis thaliana growth under salinity stress conditions

    … expression of the auxin biosynthesis gene, Nitrilase 2 (NIT2), was also specifically up-regulated in response to ionic stress. A NIT2 overexpressing line (35S::NIT2) has been shown to display improved germination and growth, as well as increased auxin levels compared to wild-type plants …

    cape-town Repository record for Investigating the molecular mechanism whereby auxin modulates Arabidopsis thaliana growth under salinity stress conditions (opens in a new tab)