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Published on: November 28, 2017
Peptide crosslinking by cytochrome P450 enzymes: Diversity, discovery and developments
Lauren A M Murray1, Alicia M Kirk2, James J De Voss3
1Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia; ARC Centre of Excellence for Innovations in Peptide and Protein Science, Clayton, VIC 3800, Australia.
Cytochrome P450 enzymes catalyze peptide cyclization reactions. These versatile enzymes show potential for engineered biocatalysis in chemoenzymatic synthesis and altering biosynthesis pathways.
Area of Science:
- Biochemistry
- Enzymology
- Synthetic Biology
Background:
- Cytochrome P450s are crucial oxidative enzymes.
- They perform diverse oxidation reactions across biological systems.
- Their role in peptide modification is an emerging area of research.
Purpose of the Study:
- To summarize recent findings on the role of Cytochrome P450s in peptide cyclization.
- To highlight the potential of P450s as biocatalysts.
- To explore their application in chemoenzymatic synthesis and metabolic engineering.
Main Methods:
- Literature review of recent studies on P450-mediated peptide cyclization.
- Analysis of P450 enzyme mechanisms in cyclization reactions.
- Discussion of engineering strategies for P450 biocatalysts.
Main Results:
- Cytochrome P450 enzymes are widely involved in the cyclization of peptides.
- These enzymes demonstrate significant versatility in catalyzing complex reactions.
- Evidence suggests P450s can be engineered for specific synthetic applications.
Conclusions:
- Cytochrome P450s play a significant role in natural peptide cyclization.
- Engineered P450s offer promising biocatalytic solutions for chemoenzymatic synthesis.
- P450s can be utilized to modify biosynthesis pathways in vivo.
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