Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium

Belcher, James; McLean, Kirsty J.; Matthews, Sarah; Woodward, L.; Fisher, Karl; Rigby, Stephen E. J.; Nelson, David R.; Potts, D. C.; Baynham, Michael T.; Parker, David; Leys, D.; Munro, Andrew W.

doi:10.1074/jbc.m113.527325

Cited by 166 publications

(228 citation statements)

References 57 publications

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“…Additionally, the crystal structure of the substrate-free form was reported (2.3 Å, PDB code: 4L54). Similar as for other CYP152 family members the carboxylate is bound by the conserved arginine (R245) [95]. The R245L OleT JE variant showed a preference for α-hydroxylation with C10:0, C12:0, and C14:0, while decarboxylation was drastically diminished.…”

Section: P450 Olet (Cyp152l1 From Jeotgalicoccus Species)mentioning

confidence: 90%

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

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Section: P450 Olet (Cyp152l1 From Jeotgalicoccus Species)mentioning

confidence: 90%

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

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“…ATCC 8456, which catalyses the oxidative decarboxylation of fatty acids to generate terminal alkenes. 115,116 OleT has a similar structure to P450 SPa and P450 BSb , including the extended loop near the conserved cysteine ligand and the presence of an arginine residue in the active site to coordinate to the carboxylate of the fatty acid. 116,117 The decarboxylation of fatty acids by OleT is supported both by peroxide and electron transfer partners, and has been extensively investigated due to the unusual nature of the reaction and the potential to use such an enzyme for biofuel production.…”

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confidence: 99%

Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism

et al. 2018

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The cytochromes P450 (P450s) are a superfamily of heme-containing monooxygenases that perform diverse catalytic roles in many species, including bacteria. The P450 superfamily is widely known for the hydroxylation of unactivated C-H bonds, but the diversity of reactions that P450s can perform vastly exceeds this undoubtedly impressive chemical transformation. Within bacteria, P450s play important roles in many biosynthetic and biodegradative processes that span a wide range of secondary metabolite pathways and present diverse chemical transformations. In this review, we aim to provide an overview of the range of chemical transformations that P450 enzymes can catalyse within bacterial secondary metabolism, with the intention to provide an important resource to aid in understanding of the potential roles of P450 enzymes within newly identified bacterial biosynthetic pathways. 1.Introduction to P450s 2.Chemistry of P450 enzymes 3.Bacterial biosynthesis pathways involving P450s 3.1Terpene metabolism 3.1. Battersby (1925Battersby ( -2018 to the molecular understanding of biosynthesis over the course of their careers.

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“…The structure and catalytic mechanism of OleT JE have been characterized (10)(11)(12), revealing how the fatty acid carboxylate binds close to the P450 heme ( Figure 1B), as well as the different mechanisms by which OleT JE produces alkenes and hydroxylated fatty acids. OleT JE was reported to catalyse 97% conversion of 200 µM myristic acid (C14:0) in the presence of 500 µM H 2 O 2 (7).…”

Section: Introductionmentioning

confidence: 99%

Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems

et al. 2017

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Jeotgalicoccus sp. 8456 OleT JE (CYP152L1) 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 OleT JE . AldO oxidizes polyols (including glycerol), generating H 2 O 2 as a co-product and facilitating its use for efficient OleT JE -dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H 2 O 2 supply to minimise 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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Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium

Cited by 166 publications

References 57 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism

Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems

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Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium

Cited by 166 publications

References 57 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism

Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2‐generating fusion protein systems

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Product

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Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems