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Production of alkenes and novel secondary products by P450 Ole T JE using novel H 2 O 2 ‐generating fusion protein systems
Author(s) -
Matthews Sarah,
Tee Kang Lan,
Rattray Nicholas J.,
McLean Kirsty J.,
Leys David,
Parker David A.,
Blankley Richard T.,
Munro Andrew W.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12581
Subject(s) - chemistry , myristic acid , streptomyces coelicolor , substrate (aquarium) , decarboxylation , oxidative decarboxylation , fatty acid , stereochemistry , biochemistry , organic chemistry , combinatorial chemistry , catalysis , palmitic acid , mutant , gene , oceanography , geology
Jeotgalicoccus sp. 8456 Ole T JE ( CYP 152L1) is a fatty acid decarboxylase cytochrome P450 that uses hydrogen peroxide (H 2 O 2 ) 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 Ole T JE . AldO oxidizes polyols (including glycerol), generating H 2 O 2 as a coproduct and facilitating its use for efficient Ole T JE ‐dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H 2 O 2 supply to minimize oxidative inactivation of Ole T 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 Ole T JE .