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dc.contributor.author Kaderbhai, Naheed N.
dc.contributor.author Kaderbhai, Mustak A.
dc.contributor.author Kelly, Steven L.
dc.date.accessioned 2009-07-21T11:09:22Z
dc.date.available 2009-07-21T11:09:22Z
dc.date.issued 2006
dc.identifier.citation Kaderbhai , N N , Kaderbhai , M A & Kelly , S L 2006 , ' Towards engineered topogenesis of cytochrome b5 and P450 for in vivo transformation of xenobiotics ' . in 8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology . pp. 1231-1235 , 8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology , Swansea , United Kingdom , 23-27 July . en
dc.identifier.citation conference en
dc.identifier.other PURE: 660273
dc.identifier.other dspace: 2160/2688
dc.identifier.uri http://hdl.handle.net/2160/2688
dc.identifier.uri http://www.biochemsoctrans.org/bst/034/1231/0341231.pdf en
dc.description Kaderbhai, M. A., Kelly, S. L., Kaderbhai, N. N. (2006).. Towards engineered topogenesis of cytochrome b5 and P450 for in vivo transformation of xenobiotics . Biochemical Society Transactions. 8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology, 34, (6), 1231-1235. 8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology en
dc.description.abstract Nature is endowed with catalysts capable of an unprecedented diversity of biotransformations, beyond the capabilities of synthetic chemistries. In a biotechnological context, there is a growing and emerging need to tap this catalytic potential. CYP (cytochrome P450) represents a superfamily of enzymes capable of a diverse array of catalytic activities. Distinct members are engaged in biosynthetic reactions within many organisms, while others have a role in the detoxification of foreign compounds. The latter substrates include medicines, pollutants, pesticides, carcinogens, perfumes and herbicides, representing considerable applied importance for pharmacology and toxicology. CYPs show a high degree of stereo- and regio-specificity for their reactions, which have wide industrial applications. Recombinant CYPs are commonly expressed as active recombinant cytosolic forms in Escherichia coli. However, selective permeability of E. coli to many substrates and products can cause problems with product recovery when using whole-cell systems. To overcome these problems, we have been developing approaches to facilitate export of functional recombinant haemoproteins to the inner membrane, periplasm and the outer membrane of E. coli. Here, we describe the progress in relation to cytochrome b5 and CYPs. en
dc.format.extent 5 en
dc.language.iso eng
dc.relation.ispartof 8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology en
dc.title Towards engineered topogenesis of cytochrome b5 and P450 for in vivo transformation of xenobiotics en
dc.type Text en
dc.type.publicationtype Conference proceeding en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en


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