9RXH
Cytochrome P450 decarboxylase from Staphylococcus aureus (OleT_Sa) with elaidic acid and acetate bound
Summary for 9RXH
| Entry DOI | 10.2210/pdb9rxh/pdb |
| Descriptor | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, Elaidic acid, ... (5 entities in total) |
| Functional Keywords | p450, peroxygenase, decarboxylase, staphylococcus aureus, decoy molecule, oxidoreductase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 50602.47 |
| Authors | |
| Primary citation | Williams, L.J.,Wilson, M.T.,Birrell, J.A.,Lang, H.W.,Bell, S.G.,Worrall, J.A.R. The cytochrome P450 decarboxylase from Staphylococcus aureus can produce a diene from a C18 monounsaturated fatty acid: A spectroscopic, structural and kinetic characterisation. J.Inorg.Biochem., 275:113117-113117, 2025 Cited by PubMed Abstract: Certain members of the bacterial cytochrome P450 152 family (CYP152) are peroxygenases that catalyse the decarboxylation of fatty acids into terminal olefins making them attractive biocatalysts for biofuel production. To date, the characterisation of decarboxylating CYP152s has mainly focused on their reaction with saturated fatty acid substrates. CYP152s are often co-purified with a bound substrate, which is generally removed before further experiments are conducted. In the present work we identified that heterologous over-expressed CYP152 from Staphylococcus aureus (OleT) is co-purified with the trans-monounsaturated C fatty acid, elaidic acid. We report the spectral, thermodynamic and kinetic characteristics of OleT bound to both elaidic acid and its saturated counterpart, stearic acid. Despite differing spectral profiles, metabolic and kinetic studies reveal that OleT is capable of decarboxylating elaidic acid, converting it to heptadeca-1,8-diene following addition of hydrogen peroxide, at the same rate and chemoselectivity as the conversion of stearic acid to 1-heptadecane. The X-ray crystal structure of the as purified OleT in complex with elaidic acid is also presented, allowing for several key residues to be identified for site-directed mutagenesis studies. The influence of the site-directed variants on C and C product formation, binding thermodynamics and kinetics have been investigated, showing that while spectral differences occur as a likely result of perturbing the binding pocket, this does not alter the chemoselectivity of the enzyme. Our work provides important insights into the mechanism of decarboxylation of an unsaturated fatty acid substrate by OleT potentially expanding the sustainable substrate space available for CYP152s. PubMed: 41125001DOI: 10.1016/j.jinorgbio.2025.113117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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