Advertisement

Applied Microbiology and Biotechnology

, Volume 59, Issue 4–5, pp 449–454 | Cite as

P450camr, a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor

  •  G. Grogan
  •  G. Roberts
  •  S. Parsons
  •  N. Turner
  •  S. Flitsch
Original Paper

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.

Keywords

Enzyme Carbon Source Molecular Mass Pseudomonas Sole Carbon Source 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Springer-Verlag 2002

Authors and Affiliations

  •  G. Grogan
    • 1
  •  G. Roberts
    • 1
  •  S. Parsons
    • 1
  •  N. Turner
    • 1
  •  S. Flitsch
    • 1
  1. 1.Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh, EH9 3JJ, UK

Personalised recommendations