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dc.contributor.author
Schapfl, Matthias
dc.contributor.author
Baier, Shiromi
dc.contributor.author
Fries, Alexander Erich
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dc.contributor.author
Ferlaino, Sascha
dc.contributor.author
Waltzer, Simon
dc.contributor.author
Müller, Michael
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dc.contributor.author
Sprenger, Georg A.
dc.date.available
2020-08-27T14:08:02Z
dc.date.issued
2018-10
dc.identifier.citation
Schapfl, Matthias; Baier, Shiromi; Fries, Alexander Erich; Ferlaino, Sascha; Waltzer, Simon; et al.; Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C–C-bonding reactions; Springer; Applied Microbiology and Biotechnology; 102; 19; 10-2018; 8359-8372
dc.identifier.issn
0175-7598
dc.identifier.uri
http://hdl.handle.net/11336/112529
dc.description.abstract
Carboligations catalyzed by aldolases or thiamine diphosphate (ThDP)-dependent enzymes are well-known in biocatalysis to deliver enantioselective chain elongation reactions. A pyruvate-dependent aldolase (2-oxo-3-deoxy-6-phosphogluconate aldolase [EDA]) introduces a chiral center when reacting with the electrophile, glyoxylic acid, delivering the (S)-enantiomer of (4S)-4-hydroxy-2-oxoglutarate [(S)-HOG]. The ThDP-dependent enzyme MenD (2-succinyl-5-enol-pyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (SEPHCHC synthase)) enables access to highly functionalized substances by forming intermolecular C?C bonds with Michael acceptor compounds by a Stetter-like 1,4- or a benzoin-condensation 1,2-addition of activated succinyl semialdehyde (ThDP adduct formed by decarboxylation of 2-oxoglutarate). MenD-catalyzed reactions are characterized by high chemo- and regioselectivity. Here, we report (S)-HOG, in situ formed by EDA, to serve as new donor substrate for MenD in 1,4-addition reactions with 2,3-trans-CHD (2,3-trans-dihydroxy-cyclohexadiene carboxylate) and acrylic acid. Likewise, (S)-HOG serves as donor in 1,2-additions with aromatic (benzaldehyde) and aliphatic (hexanal) aldehydes. This enzyme cascade of two subsequent C?C bond formations (EDA aldolase and a ThDP-dependent carboligase, MenD) generates two new stereocenters.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
1,2-ADDITIONS
dc.subject
4-HYDROXY-2-OXOGLUTARATE
dc.subject
ALDOLASE EDA
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CARBOLIGATIONS
dc.subject
MEND
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STETTER-LIKE 1,4-ADDITIONS
dc.subject
THDP-DEPENDENT ENZYME
dc.subject.classification
Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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dc.subject.classification
Biotecnología Industrial
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dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
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dc.title
Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C–C-bonding reactions
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-05-04T20:51:27Z
dc.journal.volume
102
dc.journal.number
19
dc.journal.pagination
8359-8372
dc.journal.pais
Alemania
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dc.description.fil
Fil: Schapfl, Matthias. Universität Stuttgart; Alemania
dc.description.fil
Fil: Baier, Shiromi. Universität Stuttgart; Alemania
dc.description.fil
Fil: Fries, Alexander Erich. Albert Ludwigs University of Freiburg; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Ferlaino, Sascha. Albert Ludwigs University of Freiburg; Alemania
dc.description.fil
Fil: Waltzer, Simon. Albert Ludwigs University of Freiburg; Alemania
dc.description.fil
Fil: Müller, Michael. Albert Ludwigs University of Freiburg; Alemania
dc.description.fil
Fil: Sprenger, Georg A.. Universität Stuttgart; Alemania
dc.journal.title
Applied Microbiology and Biotechnology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00253-018-9259-z
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00253-018-9259-z
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