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- Title
P450<sub>camr</sub>, a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor.
- Authors
Grogan, G.; Roberts, G. A.; Parsons, S.; Turner, N. J.; Flitsch, S. L.
- 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.
- Publication
Applied Microbiology & Biotechnology, 2002, Vol 59, Issue 4/5, p449
- ISSN
0175-7598
- Publication type
Academic Journal
- DOI
10.1007/s00253-002-1054-0