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Advances in enzymatic oxyfunctionalization of aliphatic compounds

Journal

BIOTECHNOLOGY ADVANCES
Volume 51, Issue -, Pages -

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biotechadv.2021.107703

Keywords

Peroxygenases; UPO; P450; Biocatalysis; Oxyfunctionalization; Hydroxylation; Epoxidation; Alkanes; Fatty acids; Terpenoids

Funding

  1. Bio Based Industries Joint Undertaking under the European Union [792063]
  2. Spanish Ministry of Industry, Economy and Competitiveness project [BIO2017-86559-R]
  3. FEDER funds
  4. Consejo Superior de Investigaciones Cientificas projects [PIE-201620E081, PIE-202040E185]
  5. H2020 Societal Challenges Programme [792063] Funding Source: H2020 Societal Challenges Programme

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Selective oxyfunctionalizations of aliphatic compounds are challenging chemical reactions, but enzymes such as P450 monooxygenases and unspecific peroxygenases (UPOs) play important roles due to their stereo- and regio-selectivity. UPOs, discovered in fungi, have emerged as promising biocatalysts for their ability to catalyze the oxyfunctionalization of aliphatic and aromatic compounds using only H2O2.
Selective oxyfunctionalizations of aliphatic compounds are difficult chemical reactions, where enzymes can play an important role due to their stereo- and regio-selectivity and operation under mild reaction conditions. P450 monooxygenases are well-known biocatalysts that mediate oxyfunctionalization reactions in different living organisms (from bacteria to humans). Unspecific peroxygenases (UPOs), discovered in fungi, have arisen as dream biocatalysts of great biotechnological interest because they catalyze the oxyfunctionalization of aliphatic and aromatic compounds, avoiding the necessity of expensive cofactors and regeneration systems, and only depending on H2O2 for their catalysis. Here, we summarize recent advances in aliphatic oxyfunctionalization reactions by UPOs, as well as the molecular determinants of the enzyme structures responsible for their activities, emphasizing the differences found between well-known P450s and the novel fungal peroxygenases.

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