Sterol 14alpha-demethylase activity in Streptomyces coelicolor A3(2) is associated with an unusual member of the CYP51 gene family

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dc.contributor.author Fowler, K.
dc.contributor.author Manning, Nigel J.
dc.contributor.author Lamb, David C.
dc.contributor.author Kelly, Diane E.
dc.contributor.author Kieser, T.
dc.contributor.author Podust, L. M.
dc.contributor.author Waterman, M. R.
dc.contributor.author Kelly, Steven L.
dc.date.accessioned 2009-12-15T16:39:35Z
dc.date.available 2009-12-15T16:39:35Z
dc.date.issued 2002
dc.identifier.citation Fowler , K , Manning , N J , Lamb , D C , Kelly , D E , Kieser , T , Podust , L M , Waterman , M R & Kelly , S L 2002 , ' Sterol 14alpha-demethylase activity in Streptomyces coelicolor A3(2) is associated with an unusual member of the CYP51 gene family ' Biochemical Journal , vol 364 , no. 2 , pp. 555-562 . en
dc.identifier.issn 1470-8728
dc.identifier.other PURE: 132476
dc.identifier.other dspace: 2160/3840
dc.identifier.uri http://hdl.handle.net/2160/3840
dc.description Lamb, D. C., Fowler, K., Kieser, T., Manning, N., Podust, L. M., Waterman, M. R., Kelly, D. E., Kelly, S. L. (2002). Sterol 14alpha-demethylase activity in Streptomyces coelicolor A3(2) is associated with an unusual member of the CYP51 gene family.   Biochemical Journal, 364, (2), 555-562. cytochrome P450, evolution, sterol, Streptomyces, transposon Sponsorship: BBSRC / MRC / Wellcome Trust en
dc.description.abstract The annotation of the genome sequence of Streptomyces coelicolor A3(2) revealed a cytochrome P450 (CYP) resembling various sterol 14a-demethylases (CYP51). The putative CYP open reading frame (SC7E4.20) was cloned with a tetrahistidine tag appended to the C-terminus and expressed in Escherichia coli. Protein purified to electrophoretic homogeneity was observed to bind the 14-methylated sterols lanosterol and 24-methylene-24,25-dihydrolanosterol (24-MDL). Reconstitution experiments with E. coli reductase partners confirmed activity in 14a-demethylation for 24-MDL, but not lanosterol. An S. coelicolor A3(2) mutant containing a transposon insertion in the CYP51 gene, which will abolish synthesis of the functional haemoprotein, was isolated as a viable strain, the first time a CYP51 has been identified as non-essential. The role of this CYP in bacteria is intriguing. No sterol product was detected in non-saponifiable cell extracts of the parent S. coelicolor A3(2) strain or of the mutant. S. coelicolor A3(2) CYP51 contains very few of the conserved CYP51 residues and, even though it can catalyse 14a-demethylation, it probably has another function in Streptomyces. We propose that it is a member of a new CYP51 subfamily. en
dc.format.extent 8 en
dc.language.iso eng
dc.relation.ispartof Biochemical Journal en
dc.title Sterol 14alpha-demethylase activity in Streptomyces coelicolor A3(2) is associated with an unusual member of the CYP51 gene family en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1042/BJ20011380
dc.contributor.institution Aberystwyth University en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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