Enzymatic Stetter Reaction: Computational Study of the Reaction Mechanism of MenD
Author:
Affiliation:
1. Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm SE-10691, Sweden
2. Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202, United States
Funder
Vetenskapsrådet
Publisher
American Chemical Society (ACS)
Subject
Catalysis,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acscatal.1c02292
Reference58 articles.
1. Steady-State Kinetics and Molecular Evolution of Escherichia coli MenD [(1R,6R)-2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate Synthase], an Anomalous Thiamin Diphosphate-Dependent Decarboxylase−Carboligase
2. Menaquinone Biosynthesis in Escherichia coli: Identification of 2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a Novel Intermediate and Re-Evaluation of MenD Activity
3. Determination of the Stereochemistry of 2-Succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate, a Key Intermediate in Menaquinone Biosynthesis
4. Identification and Characterization of (1R,6R)-2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate Synthase in the Menaquinone Biosynthesis of Escherichia coli
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