Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 544, Issue -, Pages 40-57Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2013.11.002
Keywords
Adenosylcobalamin; Cobalamin; Coenzyme B-12; Radical enzyme; Reactivase; Chaperone
Categories
Funding
- Japan Society for Promotion of Science
- Ministry of Education, Science, Sports and Culture, Japan
- Asahi Glass Foundation
- Nagase Science Technology Foundation
- Okayama Foundation for Science and Technology
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Adenosylcobalamin, a coenzyme form of vitamin B-12, is an organometallic compound that participates in about ten enzymatic reactions. These enzymes catalyze chemically challenging reactions by using a highly reactive primary carbon radical that is derived from homolysis of the coenzyme Co-C bond. Among them, diol dehydratases and ethanolamine ammonia-lyase have been most extensively studied to establish the general mechanism of adenosylcobalamin-assisted enzymatic catalysis and radical-catalyzed reactions. Another important point is that adenosylcobalamin-dependent radical enzymes are prone to mechanism-based irreversible inactivation during catalysis and have their own chaperones for the maintenance of catalytic activities. This review will highlight biochemical, structural, and computational studies with special emphases on radical catalysis and reactivating chaperones of these enzymes. (C) 2013 Elsevier Inc. All rights reserved.
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