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Ordered chimerogenesis applied to CYP2B P450 enzymes.

Thomas Lautier1, Philippe Urban1, Jacqueline Loeper2

  • 1Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France; CNRS, UMR5504, 135 Avenue de Rangueil, F-31400 Toulouse, France.

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Specific sequence segments in CYP2B enzymes precisely control substrate affinity shifts. Swapping elements between CYP2B6 and CYP2B11 reveals key structural determinants of enzyme function and plasticity.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • CYP2B enzymes exhibit significant structural plasticity.
  • Previous studies identified features contributing to CYP2B enzyme plasticity.

Purpose of the Study:

  • To investigate the relationship between structural elements and function in CYP2B enzymes.
  • To link shifts in substrate specificity to sequence element swaps between CYP2B6 and CYP2B11.

Main Methods:

  • Constructed 15 chimeras by swapping CYP2B6 and CYP2B11 sequence segments.
  • Assayed chimeras for substrate specificity using cyclophosphamide and 7-ethoxy-4-trifluoromethylcoumarin.
  • Determined steady-state kinetic parameters for all expressed chimeras.

Main Results:

  • Most chimeras displayed high affinity for cyclophosphamide, similar to CYP2B11.
  • Some chimeras showed affinity comparable to CYP2B6 without affecting other substrate interactions.
  • Identified specific swapped elements, including the F'/G' cassette and substrate access channels, influencing specificity shifts.

Conclusions:

  • Specific sequence segments precisely regulate cyclophosphamide affinity differences between CYP2B6 and CYP2B11.
  • This study provides a foundation for identifying structural elements that control complex enzyme functions.