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Exploring the substrate specificity of Cytochrome P450cin
Jeanette E Stok1, Peter D Giang1, Siew Hoon Wong1
1School of Chemistry and Molecular Biosciences, The University of Queensland, Australia.
Archives of Biochemistry and Biophysics
|July 30, 2019
Summary
Cytochrome P450 enzymes, like P450cin, can be engineered for selective oxidation of terpenes. Mutants N242A and N242T showed altered selectivity for monoterpenes, paving the way for biocatalytic applications.
Area of Science:
- Biochemistry
- Enzymology
- Industrial Biotechnology
Background:
- Cytochromes P450 are crucial enzymes for oxidizing diverse compounds.
- Enzyme engineering offers potential for selective substrate oxidation in biotechnology.
- P450cin and its mutants are investigated for terpene oxidation.
Purpose of the Study:
- To screen terpenes and terpenoids against P450cin and its mutants (N242A, N242T).
- To evaluate the selectivity of P450cin and its mutants in oxidizing various terpenes.
- To establish a foundation for developing novel P450cin mutants for biocatalysis.
Main Methods:
- Screening of monoterpenes and sesquiterpenes against P450cin, N242A, and N242T.
- Analysis of oxidation products using 1H NMR and GC-MS.
- Utilizing an in vivo expression system for p-cymene oxidation.
Main Results:
- P450cin oxidized most tested monoterpenes but not sesquiterpenes.
- Mutants N242A and N242T showed altered oxidation selectivity for bicyclic monoterpenes like camphor and limonene.
- P450cin uniquely oxidized p-cymene, yielding six hydroxylation products.
Conclusions:
- P450cin mutants exhibit modified substrate selectivity for monoterpenes.
- Engineered P450cin enzymes show promise for selective terpene oxidation in biocatalysis.
- Further development of P450cin mutants can enhance terpene biotransformation efficiency.
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