Structure–function analysis of the biotechnologically important cytochrome P450 107 (CYP107) enzyme family

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dc.contributor.authorSyed, Khajamohiddin
dc.contributor.authorPadayachee, Tiara
dc.contributor.authorLamb, David C.
dc.contributor.authorNelson, David R.
dc.coverageBasel, Switzerland
dc.date.accessioned2026-02-13T09:22:15Z
dc.date.available2026-02-13T09:22:15Z
dc.date.issued2023
dc.departmentNameBiochemistry and Microbiology
dc.description.abstractCytochrome P450 monooxygenases (CYPs; P450s) are a superfamily of heme-containing enzymes that are recognized for their vast substrate range and oxidative multifunctionality. CYP107 family members perform hydroxylation and epoxidation processes, producing a variety of biotechnologically useful secondary metabolites. Despite their biotechnological importance, a thorough examination of CYP107 protein structures regarding active site cavity dynamics and key amino acids interacting with bound ligands has yet to be undertaken. To address this research knowledge gap, 44 CYP107 crystal structures were investigated in this study. We demonstrate that the CYP107 active site cavity is very flexible, with ligand binding reducing the volume of the active site in some situations and increasing volume size in other instances. Polar interactions between the substrate and active site residues result in crucial salt bridges and the formation of proton shuttling pathways. Hydrophobic interactions, however, anchor the substrate within the active site. The amino acid residues within the binding pocket influence substrate orientation and anchoring, determining the position of the hydroxylation site and hence direct CYP107’s catalytic activity. Additionally, the amino acid dynamics within and around the binding pocket determine CYP107’s multifunctionality. This study serves as a reference for understanding the structure–function analysis of CYP107 family members precisely and the structure–function analysis of P450 enzymes in general. Finally, this work will aid in the genetic engineering of CYP107 enzymes to produce novel molecules of biotechnological interest.
dc.facultyFaculty of Science, Agriculture and Engineering
dc.identifier.citationPadayachee, T., Lamb, D.C., Nelson, D.R. and Syed, K., 2023. Structure–function analysis of the biotechnologically important cytochrome P450 107 (CYP107) enzyme family. Biomolecules, 13(12), pp.1-24.
dc.identifier.issn2218-273X (online)
dc.identifier.otherhttps://doi.org/10.3390/biom13121733
dc.identifier.urihttp://hdl.handle.net/10530/58703
dc.issuenumber13 / 12
dc.language.isoen
dc.pages1 - 24
dc.peerreviewedYes
dc.publisherMDPI
dc.subjectP450
dc.subjectCYP107
dc.subjectCrystal structure
dc.subjectActive site
dc.subjectEnzymatic reaction
dc.subjectSubstrate
dc.subjectSecondary metabolites
dc.subjectAmino acid dynamics
dc.subjectPolar and hydrophobic interactions
dc.titleStructure–function analysis of the biotechnologically important cytochrome P450 107 (CYP107) enzyme family
dc.title.journalBiomolecules
dc.typeJournal Article
dspace.entity.typePublication
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