Yamada Mamoru, Elias M D, Matsushita Kazunobu, Migita Catharina T, Adachi Osao
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan.
Biochim Biophys Acta. 2003 Apr 11;1647(1-2):185-92. doi: 10.1016/s1570-9639(03)00100-6.
Membrane-bound glucose dehydrogenase (mGDH) in Escherichia coli is one of the pivotal pyrroloquinoline quinone (PQQ)-containing quinoproteins coupled with the respiratory chain in the periplasmic oxidation of alcohols and sugars in Gram-negative bacteria. We compared mGDH with other PQQ-dependent quinoproteins in molecular structure and attempted to trace their evolutionary process. We also review the role of residues crucial for the catalytic reaction or for interacting with PQQ and discuss the functions of two distinct domains, radical formation in PQQ, and the presumed existence of bound quinone in mGDH.
大肠杆菌中的膜结合葡萄糖脱氢酶(mGDH)是关键的含吡咯喹啉醌(PQQ)的醌蛋白之一,在革兰氏阴性菌的周质中与呼吸链偶联,参与醇类和糖类的氧化。我们比较了mGDH与其他PQQ依赖性醌蛋白的分子结构,并试图追溯它们的进化过程。我们还综述了对催化反应或与PQQ相互作用至关重要的残基的作用,并讨论了两个不同结构域的功能、PQQ中的自由基形成以及mGDH中假定存在的结合醌。