Designing a whole-cell biotransformation system in Escherichia coli using cytochrome P450 from Streptomyces peucetius

Biotechnol Lett. 2008 Jun;30(6):1101-6. doi: 10.1007/s10529-008-9654-0. Epub 2008 Feb 8.

Abstract

A biotransformation system was designed to co-express CYP107P3 (CSP4), cytochrome P450, from Streptomyces peuceticus, along with CamA (putidaredoxin reductase) and CamB (putidaredoxin) from Pseudomonas putida, the necessary reducing equivalents, in a class I type electron-transfer system in E. coli BL21 (DE3). This was carried out using two plasmids with different selection markers and compatible origins of replication. The study results showed that this biotransformation system was able to mediate the O-dealkylation of 7-ethoxycumarin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / metabolism
  • Catalysis
  • Coumarins / metabolism
  • Cytochrome P-450 Enzyme System / metabolism*
  • Dealkylation
  • Enzyme Activation
  • Escherichia coli / enzymology
  • Escherichia coli / metabolism
  • Ferredoxins / metabolism
  • Genetic Vectors
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases / metabolism
  • Plasmids*
  • Streptomyces / enzymology*
  • Streptomyces / metabolism
  • Transformation, Bacterial*

Substances

  • Bacterial Proteins
  • Coumarins
  • Ferredoxins
  • 7-ethoxycoumarin
  • putidaredoxin
  • Cytochrome P-450 Enzyme System
  • NADH, NADPH Oxidoreductases
  • putidaredoxin reductase