Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis

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dc.identifier.uri http://dx.doi.org/10.15488/4225
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/4259
dc.contributor.author Dorival, Jonathan
dc.contributor.author Risser, Fanny
dc.contributor.author Jacob, Christophe
dc.contributor.author Collin, Sabrina
dc.contributor.author Dräger, Gerald
dc.contributor.author Paris, Cédric
dc.contributor.author Chagot, Benjamin
dc.contributor.author Kirschning, Andreas
dc.contributor.author Gruez, Arnaud
dc.contributor.author Weissman, Kira J.
dc.date.accessioned 2018-12-19T11:04:42Z
dc.date.available 2018-12-19T11:04:42Z
dc.date.issued 2018
dc.identifier.citation Dorival, J.; Risser, F.; Jacob, C.; Collin, S.; Dräger, G. et al.: Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis. In: Nature Communications 9 (2018), Nr. 1, 3998. DOI: https://doi.org/10.1038/s41467-018-06323-w
dc.description.abstract Acquisition of new catalytic activity is a relatively rare evolutionary event. A striking example appears in the pathway to the antibiotic lankacidin, as a monoamine oxidase (MAO) family member, LkcE, catalyzes both an unusual amide oxidation, and a subsequent intramolecular Mannich reaction to form the polyketide macrocycle. We report evidence here for the molecular basis for this dual activity. The reaction sequence involves several essential active site residues and a conformational change likely comprising an interdomain hinge movement. These features, which have not previously been described in the MAO family, both depend on a unique dimerization mode relative to all structurally characterized members. Taken together, these data add weight to the idea that designing new multifunctional enzymes may require changes in both architecture and catalytic machinery. Encouragingly, however, our data also show LkcE to bind alternative substrates, supporting its potential utility as a general cyclization catalyst in synthetic biology. eng
dc.language.iso eng
dc.publisher London : Nature Publishing Group
dc.relation.ispartofseries Nature Communications 9 (2018), Nr. 1
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject monoamine oxidase (MAO) eng
dc.subject LkcE eng
dc.subject catalysis eng
dc.subject.ddc 540 | Chemie ger
dc.title Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis eng
dc.type article
dc.type Text
dc.relation.issn 20411723
dc.relation.doi https://doi.org/10.1038/s41467-018-06323-w
dc.bibliographicCitation.issue 1
dc.bibliographicCitation.volume 9
dc.bibliographicCitation.firstPage 3998
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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