Adenosylcobalamin-dependent isomerases: new insights into structure and mechanism

被引：78

作者：

Marsh, ENG ^{[1
]}

Drennan, CL

机构：

[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Div Biophys, Ann Arbor, MI 48109 USA

[3] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2001年 / 5卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(00)00238-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Adenosylcobalamin-dependent isomerases catalyze a variety of chemically difficult 1,2-rearrangements that proceed through a mechanism involving free radical intermediates. These radicals are initially generated by homolysis of the cobalt-carbon bond of the coenzyme. Recently, the crystal structures of several of these enzymes have been solved, revealing two modes of coenzyme binding and highlighting the role of the protein in controlling the rearrangement of reactive substrate radical intermediates. Complementary data from kinetic, spectroscopic and theoretical studies have produced insights into the mechanism by which substrate radicals are generated at the active site, and the pathways by which they rearrange.

引用

页码：499 / 505

页数：7

共 45 条

[1] Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase [J].