Advances in enzymatic oxyfunctionalization of aliphatic compounds

Area of Science:

• Biocatalysis
• Enzymology
• Organic Chemistry

Background:

• Selective oxyfunctionalization of aliphatic compounds is challenging due to difficulties in controlling stereo- and regio-selectivity.
• Cytochrome P450 monooxygenases are established biocatalysts for oxyfunctionalization but require complex cofactor systems.
• Unspecific peroxygenases (UPOs) from fungi offer a promising alternative, catalyzing similar reactions under mild conditions.

Purpose of the Study:

• To review recent advancements in the use of UPOs for aliphatic oxyfunctionalization.
• To elucidate the structural features of UPOs that dictate their catalytic activity.
• To compare the mechanisms and properties of UPOs with those of P450 monooxygenases.

Main Methods:

• Literature review of recent studies on UPO-mediated aliphatic oxyfunctionalization.
• Analysis of structural data and mechanistic studies of UPOs.
• Comparative analysis of UPO and P450 enzyme families.

Main Results:

• UPOs demonstrate high stereo- and regio-selectivity in the oxyfunctionalization of aliphatic substrates.
• UPOs utilize hydrogen peroxide as an oxidant without the need for external cofactors or regeneration systems.
• Key structural differences between UPOs and P450s contribute to their distinct catalytic properties and substrate specificities.

Conclusions:

• UPOs represent a versatile and efficient class of biocatalysts for industrial aliphatic oxyfunctionalization.
• Understanding the molecular determinants of UPO activity can guide enzyme engineering for enhanced performance.
• UPOs offer a sustainable and cost-effective alternative to P450s for various biotechnological applications.