Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase
Evidence is presented that clavaminate synthase (CS) catalyses three oxidative reactions in the clavulanic acid biosynthetic pathway. The first CS catalysed step (hydroxylation) is separated from the latter two (oxidative cyclisation and desaturation) by the action of a hydrolytic enzyme, proclavami...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1999
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| _version_ | 1797097051504246784 |
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| author | Lloyd, MD Merritt, K Lee, V Sewell, T Wha-Son, B Baldwin, J Schofield, C Elson, S Baggaley, K Nicholson, N |
| author_facet | Lloyd, MD Merritt, K Lee, V Sewell, T Wha-Son, B Baldwin, J Schofield, C Elson, S Baggaley, K Nicholson, N |
| author_sort | Lloyd, MD |
| collection | OXFORD |
| description | Evidence is presented that clavaminate synthase (CS) catalyses three oxidative reactions in the clavulanic acid biosynthetic pathway. The first CS catalysed step (hydroxylation) is separated from the latter two (oxidative cyclisation and desaturation) by the action of a hydrolytic enzyme, proclavaminate amidinohydrolase, which modifies (or 'mutates') the sidechain of the product of the first reaction thereby converting it into a substrate for the second CS catalysed reaction. |
| first_indexed | 2024-03-07T04:50:10Z |
| format | Journal article |
| id | oxford-uuid:d4acf1c0-6c4b-4f8e-8ff4-935ef563c405 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:50:10Z |
| publishDate | 1999 |
| record_format | dspace |
| spelling | oxford-uuid:d4acf1c0-6c4b-4f8e-8ff4-935ef563c4052022-03-27T08:20:27ZProduct-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenaseJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d4acf1c0-6c4b-4f8e-8ff4-935ef563c405EnglishSymplectic Elements at Oxford1999Lloyd, MDMerritt, KLee, VSewell, TWha-Son, BBaldwin, JSchofield, CElson, SBaggaley, KNicholson, NEvidence is presented that clavaminate synthase (CS) catalyses three oxidative reactions in the clavulanic acid biosynthetic pathway. The first CS catalysed step (hydroxylation) is separated from the latter two (oxidative cyclisation and desaturation) by the action of a hydrolytic enzyme, proclavaminate amidinohydrolase, which modifies (or 'mutates') the sidechain of the product of the first reaction thereby converting it into a substrate for the second CS catalysed reaction. |
| spellingShingle | Lloyd, MD Merritt, K Lee, V Sewell, T Wha-Son, B Baldwin, J Schofield, C Elson, S Baggaley, K Nicholson, N Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title | Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title_full | Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title_fullStr | Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title_full_unstemmed | Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title_short | Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase |
| title_sort | product substrate engineering by bacteria studies on clavaminate synthase a trifunctional dioxygenase |
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