| Use this URL to cite or link to this record in EThOS: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490535 |
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| Title: | Structural studies of the prokaryotic arylamine n-acetyltransferases | ||||
| Author: | Sandy, James |
ISNI:
0000 0001 3551 3402
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| Awarding Body: | University of Salford | ||||
| Current Institution: | University of Salford | ||||
| Date of Award: | 2005 | ||||
| Availability of Full Text: |
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| Abstract: | |||||
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The arylamine iV-acetyltransferases (NATs) catalyse the transfer of an acetyl group from the co-factor acetyl CoenzymeA (acetyl CoA) onto the temiinal nitrogen of a range of arylamine and arylhydrazine compounds, including the anti-tubercular agent isoniazid. often inactivating these compounds. In order to further investigate the NAT enzymes at the molecular level a 3D structure was required.
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| Supervisor: | Not available | Sponsor: | Not available | ||
| Qualification Name: | Thesis (Ph.D.) | Qualification Level: | Doctoral | ||
| EThOS ID: | uk.bl.ethos.490535 | DOI: | Not available | ||
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