P450(camr), a cytochrome P450 catalysing the stereospecific 6- endo-hydroxylation of (1 R)-(+)-camphor

G Grogan, G A Roberts, S Parsons, N J Turner, S L Flitsch

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Rhodococcus sp. NCIMB 9784 accumulated 6- endo-hydroxycamphor 3 when grown on (1 R)-(+)-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 (1 R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6- endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1 R)-(+)-camphor specifically in the 6- endoposition, in contrast to the 5- exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.

Original languageEnglish
Pages (from-to)449-54
Number of pages6
JournalApplied Microbiology and Biotechnology
Issue number4-5
Publication statusPublished - Jun 2002

Keywords / Materials (for Non-textual outputs)

  • Camphor/chemistry
  • Crystallography, X-Ray
  • Cytochrome P-450 Enzyme System/isolation & purification
  • Electrophoresis, Polyacrylamide Gel
  • Hydroxylation
  • Models, Molecular
  • Rhodococcus/enzymology
  • Stereoisomerism


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