Study of P450 enzymes of the CYP152 family able to promote the decarboxylation of fatty acids

• Grant number: 21/14410-2
• Support Opportunities: Scholarships in Brazil - Master
• Start date: June 01, 2022
• End date: July 31, 2024
• Field of knowledge: Biological Sciences - Biochemistry - Enzymology
• Principal Investigator: Leticia Maria Zanphorlin
• Grantee: Isabelle Taira Simões
• Host Institution: Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Ministério da Ciência, Tecnologia e Inovação (Brasil). Campinas , SP, Brazil
• Associated scholarship(s): 22/13822-8 - Metabolic engineering of Yarrowia lipolytica for alkene production with P450 decarboxylases of a newly discovered cluster, BE.EP.MS

Abstract

Terminal alkenes are important compounds in the chemical industry and can be used in the production of polyethylene, detergents, surfactants and lubricants. Currently, these products are mostly produced from petroleum. However, considering the economic and environmental conflicts created by this resource, it is necessary to search for an alternative and renewable route for the production of these compounds. The cytochromes P450 are a superfamily of enzymes that, in humans, play an important role in the biotransformation of drugs and toxins. In recent years, the discovery of P450 peroxygenases from the CYP152 family has attracted great notoriety due to the ability to catalyze the removal of oxygen from medium- and long-chain fatty acids, resulting in alkene production. These enzymes, known as OleT, catalyze the production of alkenes with a double bond on the ±-carbon, from the decarboxylation of fatty acids. However, the molecular mechanisms of these peroxygenases are still unclear, as few enzymes from this family have been reported so far. Thus, this project aims to investigate new putative P450 peroxygenases with possible decarboxylase function. These genes will be chosen from a previous study based on sequence similarity networks (SSN), carried out with sequences with conserved amino acids, important for fatty acid decarboxylase activity. Thus, the proteins used will be investigated through a combination of structural, spectroscopical, biochemical and bioinformatical methods, increasing the available pool of peroxygenases with decarboxylase activity.