Identification and Characterization of Thiamine Diphosphate‐Dependent Lyases with an Unusual CDG Motif
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Identification and Characterization of Thiamine Diphosphate‐Dependent Lyases with an Unusual CDG Motif ; day:22 ; month:07 ; year:2024 ; extent:10
Angewandte Chemie / International edition. International edition ; (22.07.2024) (gesamt 10)
- Urheber
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Lanza, Lucrezia
Rabe von Pappenheim, Fabian
Bjarnesen, Daniela
Leogrande, Camilla
Paul, Alexandra
Krug, Leonhard
Tittmann, Kai
Müller, Michael
- DOI
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10.1002/anie.202404045
- URN
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urn:nbn:de:101:1-2407231415379.744117544843
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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14.08.2025, 11:00 MESZ
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Beteiligte
- Lanza, Lucrezia
- Rabe von Pappenheim, Fabian
- Bjarnesen, Daniela
- Leogrande, Camilla
- Paul, Alexandra
- Krug, Leonhard
- Tittmann, Kai
- Müller, Michael
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Mechanistic and Structural Characterization of Thiamine Diphosphate Dependent Enzyme Transketolases from Human and E.coli
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Regulatory interactions of enzymes of the citric acid cycle in Bacillus subtilis
Protein interactions along the presequence import pathway
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Identification and Characterization of Thiamine Diphosphate‐Dependent Lyases with an Unusual CDG Motif
Identification and characterization of thiamine diphosphate‐dependent lyases with an unusual cdg motif
Mechanistic and Structural Characterization of Thiamine Diphosphate Dependent Enzyme Transketolases from Human and E.coli
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Radical Phosphate Transfer Mechanism for the Thiamin Diphosphate- and FAD-Dependent Pyruvate Oxidase from Lactobacillus plantarum : Kinetic Coupling of Intercofactor Electron Transfer with Phosphate Transfer to Acetyl-thiamin Diphosphate via a Transient FAD Semiquinone/Hydroxyethyl-ThDP Radical Pair
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Protein interactions along the presequence import pathway