Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form
| dc.contributor.author | Thuku, R Ndoria | |
| dc.contributor.author | Weber, Brandon W | |
| dc.contributor.author | Varsani, Arvind | |
| dc.contributor.author | Sewell, B. Trevor | |
| dc.date.accessioned | 2016-09-05T18:44:50Z | |
| dc.date.available | 2016-09-05T18:44:50Z | |
| dc.date.issued | 2007 | |
| dc.date.updated | 2016-09-05T13:16:18Z | |
| dc.description.abstract | Nitrilases convert nitriles to the corresponding carboxylic acids and ammonia. The nitrilase from Rhodococcus rhodochrous J1 is known to be inactive as a dimer but to become active on oligomerization. The recombinant enzyme undergoes post-translational cleavage at approximately residue 327, resulting in the formation of active, helical homo-oligomers. Determining the 3D structure of these helices using electron microscopy, followed by fitting the stain envelope with a model based on homology with other members of the nitrilase superfamily, enables the interacting surfaces to be identified. This also suggests that the reason for formation of the helices is related to the removal of steric hindrance arising from the 39 C-terminal amino acids from the wild-type protein. The helical form can be generated by expressing only residues 1-327. | en_ZA |
| dc.identifier | http://dx.doi.org/10.1111/j.1742-4658.2007.05752.x | |
| dc.identifier.apacitation | Thuku, R. N., Weber, B. W., Varsani, A., & Sewell, B. Trevor. (2007). Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form. <i>FEBS Journal</i>, http://hdl.handle.net/11427/21672 | en_ZA |
| dc.identifier.chicagocitation | Thuku, R Ndoria, Brandon W Weber, Arvind Varsani, and B. Trevor Sewell "Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form." <i>FEBS Journal</i> (2007) http://hdl.handle.net/11427/21672 | en_ZA |
| dc.identifier.citation | Thuku, R. N., Weber, B. W., Varsani, A., & Sewell, B. T. (2007). Post‐translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form. FEBS Journal, 274(8), 2099-2108. | en_ZA |
| dc.identifier.issn | 1742-464X | en_ZA |
| dc.identifier.ris | TY - Journal Article AU - Thuku, R Ndoria AU - Weber, Brandon W AU - Varsani, Arvind AU - Sewell, B. Trevor AB - Nitrilases convert nitriles to the corresponding carboxylic acids and ammonia. The nitrilase from Rhodococcus rhodochrous J1 is known to be inactive as a dimer but to become active on oligomerization. The recombinant enzyme undergoes post-translational cleavage at approximately residue 327, resulting in the formation of active, helical homo-oligomers. Determining the 3D structure of these helices using electron microscopy, followed by fitting the stain envelope with a model based on homology with other members of the nitrilase superfamily, enables the interacting surfaces to be identified. This also suggests that the reason for formation of the helices is related to the removal of steric hindrance arising from the 39 C-terminal amino acids from the wild-type protein. The helical form can be generated by expressing only residues 1-327. DA - 2007 DB - OpenUCT DP - University of Cape Town J1 - FEBS Journal LK - https://open.uct.ac.za PB - University of Cape Town PY - 2007 SM - 1742-464X T1 - Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form TI - Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form UR - http://hdl.handle.net/11427/21672 ER - | en_ZA |
| dc.identifier.uri | http://hdl.handle.net/11427/21672 | |
| dc.identifier.vancouvercitation | Thuku RN, Weber BW, Varsani A, Sewell B Trevor. Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form. FEBS Journal. 2007; http://hdl.handle.net/11427/21672. | en_ZA |
| dc.language | eng | en_ZA |
| dc.publisher | Wiley | en_ZA |
| dc.publisher.institution | University of Cape Town | |
| dc.rights | Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) | * |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc/4.0/ | en_ZA |
| dc.source | FEBS Journal | en_ZA |
| dc.source.uri | http://febs.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1742-4658/ | |
| dc.subject.other | electron microscopy | |
| dc.subject.other | helix | |
| dc.subject.other | IHRSR | |
| dc.subject.other | nitrilase | |
| dc.subject.other | oligomeric form | |
| dc.title | Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form | en_ZA |
| dc.type | Journal Article | en_ZA |
| uct.type.filetype | Text | |
| uct.type.filetype | Image | |
| uct.type.publication | Research | en_ZA |
| uct.type.resource | Article | en_ZA |