A New Class of EutT ATP:Co(I)rrinoid Adenosyltransferases Found in Listeria monocytogenes and Other Firmicutes Does Not Require a Metal Ion for Activity
Author:
Affiliation:
1. Department of Microbiology, University of Georgia, 212C Biological Sciences Building, 120 Cedar Street, Athens, Georgia 30602, United States
Funder
U.S. Department of Health and Human Services
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00715
Reference47 articles.
1. Radical Carbon Skeleton Rearrangements: Catalysis by Coenzyme B12-Dependent Mutases
2. Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12
3. Spectroscopic Evidence for the Formation of a Four-Coordinate Co2+Cobalamin Species upon Binding to the Human ATP:Cobalamin Adenosyltransferase
4. Spectroscopic and Computational Studies of the ATP:Corrinoid Adenosyltransferase (CobA) from Salmonella enterica: Insights into the Mechanism of Adenosylcobalamin Biosynthesis
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2. Localization and interaction studies of the Salmonella enterica ethanolamine ammonia‐lyase ( EutBC ), its reactivase ( EutA ), and the EutT corrinoid adenosyltransferase;Molecular Microbiology;2022-07-18
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4. The Cobalamin-Dependent Gene Cluster of Listeria monocytogenes: Implications for Virulence, Stress Response, and Food Safety;Frontiers in Microbiology;2020-11-06
5. Replacement of the Cobalt Center of Vitamin B 12 by Nickel: Nibalamin and Nibyric Acid Prepared from Metal‐Free B 12 Ligands Hydrogenobalamin and Hydrogenobyric Acid;Angewandte Chemie International Edition;2020-09-02
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