P450(camr), a cytochrome P450 catalysing the stereospecific 6- endo-hydroxylation of (1 R)-(+)-camphor |
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| Authors: | Grogan G Roberts G A Parsons S Turner N J Flitsch S L |
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| Institution: | (1) Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh, EH9 3JJ, UK,;(2) Present address: York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK, |
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| Abstract: | Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)-camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using X-ray crystallography. A soluble cytochrome P450 hydroxylase, induced
by growth on (1R)-(+)-camphor and designated P450camr, has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450camr and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450cam from P. putida. P450camr has a molecular mass of approximately 44 kDa, and a pI of 4.8.
Electronic Publication |
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