Journal
FEBS LETTERS
Volume 591, Issue 5, Pages 737-750Publisher
WILEY
DOI: 10.1002/1873-3468.12581
Keywords
alkene production; CYP152L1; cytochrome P450; fusion enzymes; hydrogen peroxide; OleT(JE) peroxygenase
Funding
- UK Biotechnology and Biological Sciences Research Council (BBSRC)
- BBSRC/Shell UK Ltd [BB/N006275/1, BB/K017802/1]
- BBSRC
- Agilent Technologies UK Ltd [BB/J012645/1]
- BBSRC [BB/N006275/1, BB/M017702/1, BB/K017802/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/N006275/1, BB/M017702/1, 1225743, BB/K017802/1] Funding Source: researchfish
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Jeotgalicoccus sp. 8456 OleT(JE) (CYP152L1) is a fatty acid decarboxylase cytochrome P450 that uses hydrogen peroxide (H2O2) to catalyse production of terminal alkenes, which are industrially important chemicals with biofuel applications. We report enzyme fusion systems in which Streptomyces coelicolor alditol oxidase (AldO) is linked to OleT(JE). AldO oxidizes polyols (including glycerol), generating H2O2 as a coproduct and facilitating its use for efficient OleT(JE)-dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H2O2 supply to minimize oxidative inactivation of OleT(JE) and prolong activity for increased alkene production. We also use these fusion systems to generate novel products from secondary turnover of 2-OH and 3-OH myristic acid primary products, expanding the catalytic repertoire of OleT(JE).
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