Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential

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dc.identifier.uri http://dx.doi.org/10.15488/123
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/141
dc.contributor.author Abood, Amira
dc.contributor.author Al-Fahad, Ahmed
dc.contributor.author Scott, Alan
dc.contributor.author Hosny, Alaa El-Dein M. S.
dc.contributor.author Hashem, Amal M.
dc.contributor.author Fattah, Azza M.A.
dc.contributor.author Race, Paul R.
dc.contributor.author Simpson, Thomas J.
dc.contributor.author Cox, Russell J.
dc.date.accessioned 2015-12-03T10:13:26Z
dc.date.available 2015-12-03T10:13:26Z
dc.date.issued 2015-05-29
dc.identifier.citation Abood, Amira; Al-Fahad, Ahmed; Scott, Alan; Hosny, Alaa El-Dein M. S.; Hashem, Amal M.; Fattah, Azza M. A.; Race, Paul R.; Simpson, Thomas J.; Cox, Russell J.: Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential. In: Rsc Advances 5 (2015), Nr. 62, S. 49987-49995. DOI: http://dx.doi.org/10.1039/c5ra06693j
dc.description.abstract Achieving regio-specific hydroxylation of aromatic compounds remains a major challenge in synthetic chemistry. By contrast, this transformation is readily accomplished in nature through the action of FAD-dependant monooxygenase enzymes. Here, we report the kinetic characterisation of one such enzyme, TropB, from the stipitatic acid biosynthetic pathway. Analogues of the TropB natural substrate, 3-methyl-orcinaldehyde, were synthesised and used to examine the substrate selectivity of this enzyme. TropB displays broad substrate tolerance, for instance accepting single-ring aromatic substrates containing a range of C-1 substituents with varying electronic and steric properties. These include nitro, nitrosyl, alkyl, and aryl keto groups. Bicyclic substrates, however, were rejected by TropB. Additionally, C-5 substituents on single-ring aromatic substrates were not tolerated whereas the presence of a 6-methyl group was found to be important for substrate binding. Docking studies were employed to investigate and understand the broad substrate selectivity of TropB and identifies the key structural elements of its substrates. Our work has shown that TropB is an attractive target for biocatalyst engineering and industrial aromatic hydroxylation. eng
dc.description.sponsorship Al Baha University, Saudi Arabia
dc.description.sponsorship EP/F066104/1
dc.description.sponsorship BB/I003355/1
dc.language.iso eng eng
dc.publisher Cambridge : Royal Society of Chemistry
dc.relation.ispartofseries RSC Advances 5 (2015), Nr. 62
dc.rights CC BY 3.0 Unported
dc.rights.uri http://creativecommons.org/licenses/by/3.0/
dc.subject swiss-model eng
dc.subject oxidative dearomatization eng
dc.subject mesorhizobium-loti eng
dc.subject biosynthesis eng
dc.subject electrostatics eng
dc.subject hydroxylation eng
dc.subject nitration eng
dc.subject phenol eng
dc.subject.ddc 540 | Chemie ger
dc.title Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential eng
dc.type article
dc.type Text
dc.relation.issn 2046-2069
dc.relation.doi http://dx.doi.org/10.1039/c5ra06693j
dc.bibliographicCitation.issue 62
dc.bibliographicCitation.volume 5
dc.bibliographicCitation.firstPage 49987
dc.bibliographicCitation.lastPage 49995
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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