Show simple item record Jackson, Colin J. Lamb, David Christopher Marczylo, Timothy H. Parker, Josie E. Manning, Nigel L. Kelly, Diane Elizabeth Kelly, Steven Lewis 2010-03-09T14:52:16Z 2010-03-09T14:52:16Z 2003-02-07
dc.identifier.citation Jackson , C J , Lamb , D C , Marczylo , T H , Parker , J E , Manning , N L , Kelly , D E & Kelly , S L 2003 , ' Conservation and cloning of CYP51: a sterol 14 alpha-demethylase from Mycobacterium smegmatis ' Biochemical and Biophysical Research Communications , vol 301 , no. 2 , pp. 558-563 . DOI: 10.1016/S0006-291X(02)03078-4 en
dc.identifier.issn 0006-291X
dc.identifier.other PURE: 137849
dc.identifier.other PURE UUID: 8ebc75cb-3ab2-400d-9058-650dedcba851
dc.identifier.other dspace: 2160/4205
dc.identifier.other DSpace_20121128.csv: row: 3131
dc.identifier.other Scopus: 0037423691
dc.description Jackson, C. J., Lamb, D. C., Marczylo, T. H., Parker, J. E., Manning, N. L., Kelly, D. E., Kelly, S. L. (2003). Conservation and cloning of CYP51: a sterol 14 alpha-demethylase from Mycobacterium smegmatis. Biochemical and Biophysical Research Communications, 30301, (2), 558-563. Sponsorship: BBSRC en
dc.description.abstract The genetic locus encoding cytochrome P450 51 (CYP51; P45014DM) in Mycobacterium smegmatis is described here together with confirmation of activity in lanosterol 14α-demethylation. The protein bound azole antifungals with high affinity and the rank order based on affinity matched the ranked order for microbiological sensitivity of the organism, thus supporting a possible role for CYP51 as a target in the antimycobacterial activity of these compounds. Non-saponifiable lipids were extracted from the bacteria grown on minimal medium. Unlike a previous report using growth on complex medium, no cholesterol was detected in two strains of M. smegmatis, but a novel lipid was detected. The genetic locus of CYP51 is discussed in relation to function; it is conserved as part of a putative operon in M. smegmatis, Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium bovis and consists of six open-reading frames including two CYPs and a ferredoxin under a putative Tet-R regulated promoter. en
dc.format.extent 6 en
dc.language.iso eng
dc.relation.ispartof Biochemical and Biophysical Research Communications en
dc.rights en
dc.subject cytochrome P450 en
dc.subject Sterol 14-demethylase en
dc.subject Azole en
dc.subject Mycobacteria en
dc.title Conservation and cloning of CYP51: a sterol 14 alpha-demethylase from Mycobacterium smegmatis en
dc.type /dk/atira/pure/researchoutput/researchoutputtypes/contributiontojournal/article en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en

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