Structure and Mutational Analysis of the Archaeal GTP:AdoCbi-P Guanylyltransferase (CobY) from Methanocaldococcus jannaschii: Insights into GTP Binding and Dimerization
Author:
Affiliation:
1. Department of Biochemistry and ‡Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi200329t
Reference50 articles.
1. Radical Carbon Skeleton Rearrangements: Catalysis by Coenzyme B12-Dependent Mutases
2. How a Protein Binds B 12 : A 3.0 Å X-Ray Structure of B 12 -Binding Domains of Methionine Synthase
3. Crystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and Substrates
4. Radical Catalysis in Coenzyme B12-Dependent Isomerization (Eliminating) Reactions
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1. Structural studies of the phosphoribosyltransferase involved in cobamide biosynthesis in methanogenic archaea and cyanobacteria;Scientific Reports;2022-10-13
2. New Insights Into the Biosynthesis of Cobamides and Their Use;Comprehensive Natural Products III;2020
3. Cobalamin Biosynthesis and Insertion;Encyclopedia of Inorganic and Bioinorganic Chemistry;2017-09-15
4. Microbial production of vitamin B12: a review and future perspectives;Microbial Cell Factories;2017-01-30
5. Solution Structural Studies of GTP:Adenosylcobinamide-Phosphateguanylyl Transferase (CobY) from Methanocaldococcus jannaschii;PLOS ONE;2015-10-29
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