Computational Study on Mechanistic Details of the Aminoethanol Rearrangement Catalyzed by the Vitamin B12-Dependent Ethanolamine Ammonia Lyase: His and Asp/Glu Acting Simultaneously as Catalytic Auxiliaries
Author:
Affiliation:
1. Contribution from the Institut für Chemie der Technischen Universität Berlin, D-10623 Berlin, Germany
Publisher
American Chemical Society (ACS)
Subject
Organic Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jo0301705
Reference61 articles.
1. The Clostridial Fermentations of Choline and Ethanolamine
2. 5‘-Deoxyadenosine Contacts the Substrate Radical Intermediate in the Active Site of Ethanolamine Ammonia-lyase: 2H and 13C Electron Nuclear Double Resonance Studies
3. The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Evidence that the hydrogen transfer mechanism involves a second intermediate hydrogen carrier in addition to the cofactor.
4. Identification of a Rearranged-Substrate, Product Radical Intermediate and the Contribution of a Product Radical Trap in Vitamin B12 Coenzyme-Dependent Ethanolamine Deaminase Catalysis
5. Identification of a Rearranged-Substrate, Product Radical Intermediate and the Contribution of a Product Radical Trap in Vitamin B12 Coenzyme-Dependent Ethanolamine Deaminase Catalysis
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