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

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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Toraya T

doi

10.1016/j.abb.2013.11.002

subject

Has Abstract

pub_date

2014-02-15 00:00:00

pages

40-57

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(13)00348-2

journal_volume

544

pub_type

杂志文章,评审

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