Applied Microbiology and Biotechnology

, Volume 97, Issue 4, pp 1625–1635 | Cite as

Cytochrome P450 reductase from Candida apicola: versatile redox partner for bacterial P450s

  • Marco Girhard
  • Florian Tieves
  • Evelyne Weber
  • Martha Sophia Smit
  • Vlada B. Urlacher
Biotechnologically relevant enzymes and proteins


Candida apicola belongs to a group of yeasts producing surface-active glycolipids consisting of sophorose and long-chain (ω)- or (ω-1)-hydroxy fatty acids. Hydroxylation of the fatty acids in this strain is likely catalyzed by cytochrome P450 monooxygenases (P450), which require reducing equivalents delivered via a cytochrome P450-diflavin reductase (CPR). We herein report cloning and characterization of the cpr gene from C. apicola ATCC 96134. The gene encoding a protein of 687 amino acids was cloned in Escherichia coli and the enzyme was expressed in functional form after truncation of its N-terminal putative membrane anchor. The truncated recombinant protein showed cytochrome c reducing activity (KM of 13.8 μM and kcat of 1,915 per minute). Furthermore, we herein demonstrate to our best knowledge for the first time the use of a eukaryotic CPR to transfer electrons to bacterial P450s (namely CYP109B1 and CYP154E1). Cloning and characterization of this CPR therefore is not only an important step in the study of the P450 systems of C. apicola, but also provides a versatile redox partner for the characterization of other bacterial P450s with appealing biotechnological potential. The GenBank accession number of the sequence described in this article is JQ015264.


Candida apicola Cytochrome P450-diflavin reductase CPR P450 Heterologous expression 

Supplementary material

253_2012_4026_MOESM1_ESM.pdf (330 kb)
ESM 1(PDF 330 kb)


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Copyright information

© Springer-Verlag 2012

Authors and Affiliations

  • Marco Girhard
    • 1
  • Florian Tieves
    • 1
  • Evelyne Weber
    • 2
  • Martha Sophia Smit
    • 3
  • Vlada B. Urlacher
    • 1
  1. 1.Institute of BiochemistryHeinrich-Heine University DüsseldorfDüsseldorfGermany
  2. 2.Institute of Technical BiochemistryUniversität StuttgartStuttgartGermany
  3. 3.Department of Microbial, Biochemical and Food BiotechnologyUniversity of the Free StateBloemfonteinSouth Africa

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