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Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61
Includes bibliographical references.
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| Other Authors: | |
| Format: | Thesis |
| Language: | English |
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Department of Molecular and Cell Biology
2016
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| _version_ | 1867613250208661504 |
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| access_status_str | Open Access |
| author | Berman, Mark Nicholas |
| author2 | Sewell, Bryan Trevor |
| author_browse | Berman, Mark Nicholas Sewell, Bryan Trevor |
| author_facet | Sewell, Bryan Trevor Berman, Mark Nicholas |
| author_sort | Berman, Mark Nicholas |
| collection | Thesis |
| description | Includes bibliographical references. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/17877 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:33:08.525Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2016 |
| publishDateRange | 2016 |
| publishDateSort | 2016 |
| publisher | Department of Molecular and Cell Biology |
| publisherStr | Department of Molecular and Cell Biology |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/17877 Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 Berman, Mark Nicholas Sewell, Bryan Trevor Meyers, Paul Molecular and Cell Biology Includes bibliographical references. Nitrilases catalyse the conversion of a nitrile to its corresponding acid and ammonia by the addition of two water molecules. Cyanide dihydratases, a subgroup of nitrilases, specifically hydrolyse cyanide to formic acid and ammonia. Nitrilases are found in a diverse collection organisms that includes plants, bacteria and fungi. They form one branch a superfamily of structurally related enzymes that are believed to have in common a unique cys-glu-Iys catalytic triad. Many nitrilases exiat as a large molecular weight oligomers of more than 300kDa. In the current study the structures of two cyanide dihydratases, from Pseudomonas stutzeri AK61 and Bacillus pumilus Cl, have solved at a resolution 2.9nm and 32nm respectively by single particle reconstruction from electron micrographs of enzyme particles stained in uranyl acetate. Each enzyme consists of a spiral structure of well-defined length. It is proposed that this arrangement of subunits occurs in many other nitrilases and that a number of unexplained observations in the literature can reconciled by this model. 2016-03-17T07:12:03Z 2016-03-17T07:12:03Z 2003 Master Thesis Masters MSc http://hdl.handle.net/11427/17877 eng application/pdf Department of Molecular and Cell Biology Faculty of Science University of Cape Town |
| spellingShingle | Molecular and Cell Biology Berman, Mark Nicholas Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| thesis_degree_str | Master's |
| title | Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| title_full | Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| title_fullStr | Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| title_full_unstemmed | Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| title_short | Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 |
| title_sort | quaternary structures of the cyanide dihydratases of bacillus pumilus c1 and pseudomonas stutzeri ak61 |
| topic | Molecular and Cell Biology |
| url | http://hdl.handle.net/11427/17877 |
| work_keys_str_mv | AT bermanmarknicholas quaternarystructuresofthecyanidedihydratasesofbacilluspumilusc1andpseudomonasstutzeriak61 |