Structure and mechanism of soluble glucose dehydrogenase and other PQQ-dependent enzymes

被引：49
作者：
Oubrie, A [1 ]
机构：
[1] Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2003年 / 1647卷 / 1-2期
关键词：
bacterial evolution; catalytic mechanism; crystal structure; glucose dehydrogenase; hydride transfer; quinoprotein;
D O I：
10.1016/S1570-9639(03)00087-6
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：
This paper discusses recent X-ray structures of several pyrroloquinoline quinone (PQQ)-dependent proteins in relation to their proposed modes of action. In addition, a detailed analysis of redox-related structural changes in the soluble PQQ-dependent glucose dehydrogenase is presented. A sequence comparison of that enzyme with a number of homologues shows that PQQ-dependent enzymes are much more widespread than has been assumed so far. In particular, the presence of a PQQ-dependent enzyme in at least one archaeon opens up the possibility that PQQ has been involved in prokaryotic metabolism since the early days of the evolution of bacterial life on earth. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码：143 / 151
页数：9
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