Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases

被引:63
作者
Edwards, KJ
Barton, JD
Rossjohn, J
Thorn, JM
Taylor, GL
Ollis, DL
机构
[1] ST VINCENTS INST MED RES, FITZROY, VIC 3065, AUSTRALIA
[2] UNIV BATH, SCH BIOL & BIOCHEM, BATH BA2 7AY, AVON, ENGLAND
关键词
alcohol dehydrogenase; glucose dehydrogenase; medium chain dehydrogenase; quinone oxido-reductase; zeta-crystallin;
D O I
10.1006/abbi.1996.0158
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
Quinone oxidoreductase, xi-crystallin, glucose dehydrogenase, and alcohol dehydrogenase belong to a superfamily of medium-chain dehydrogenase/reductases, The crystal structures of Escherichia coli quinone oxidoreductase (QOR) and Thermoplasma acidophilun glucose dehydrogenase have recently been determined and are compared here with the well-known structure of horse liver alcohol dehydrogenase. A structurally based comparison of these three enzymes confirms that they possess extensive overall structural homology despite low sequence identity, The most significant difference is the absence of the catalytic and structural zinc ions in QOR, A multiple structure-based sequence alignment has been constructed for the three enzymes and extended to include xi-crystallin, an eye lens structural protein with quinone oxidereductase activity and high sequence identity to E. coli quinone oxidoreductase. Residues which are important for catalysis have been altered and the functions and activities of the enzymes have diverged, illustrating a classic example of divergent evolution among a superfamily of enzymes, (C) 1996 Academic Press, Inc.
引用
收藏
页码:173 / 183
页数:11
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