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Arch Biochem Biophys. 2014 Feb 15;544:40-57. doi: 10.1016/j.abb.2013.11.002. Epub 2013 Nov 19.

Cobalamin-dependent dehydratases and a deaminase: radical catalysis and reactivating chaperones.

Author information

1
Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Japan. Electronic address: toraya@cc.okayama-u.ac.jp.

Abstract

Adenosylcobalamin, a coenzyme form of vitamin B12, 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.

KEYWORDS:

Adenosylcobalamin; Chaperone; Cobalamin; Coenzyme B(12); Radical enzyme; Reactivase

PMID:
24269950
DOI:
10.1016/j.abb.2013.11.002
[Indexed for MEDLINE]

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