Nakamura K, GO N
Quantum Bioinformatics Group. Center for Promotion of Computational Science and Engineering, Japan Atomic Energy Research Institute, 801, Umemidai Soraku-gun, Kyoto 619-0215, Japan.
Cell Mol Life Sci. 2005 Sep;62(18):2050-66. doi: 10.1007/s00018-004-5076-x.
Multicopper blue proteins (MCBPs) are multidomain proteins that utilize the distinctive redox ability of copper ions. There are a variety of MCBPs that have been roughly classified into three different groups, based on their domain organization and functions: (i) nitrite reductase-type with two domains, (ii) laccase-type with three domains, and (iii) ceruloplasmin-type with six domains. Together, the second and third group are often commonly called multicopper oxidases (MCOs). The rapid accumulation of genome sequence information in recent years has revealed several new types of proteins containing MCBP domains, mainly from bacteria. In this review, the recent research on the functions and structures of MCBPs is summarized, mainly focusing on the new types. The latter half of this review focusses on the two domain MCBPs, which we propose as the evolutionary intermediate of the MCBP family.
多铜蓝蛋白（MCBPs）是利用铜离子独特氧化还原能力的多结构域蛋白。根据其结构域组织和功能，有多种MCBPs大致可分为三个不同的组：（i）具有两个结构域的亚硝酸还原酶型，（ii）具有三个结构域的漆酶型，以及（iii）具有六个结构域的铜蓝蛋白型。第二组和第三组合在一起通常被称为多铜氧化酶（MCOs）。近年来基因组序列信息的快速积累揭示了几种含有MCBP结构域的新型蛋白质，主要来自细菌。在本综述中，总结了MCBPs功能和结构的最新研究，主要聚焦于新型。本综述的后半部分聚焦于两个结构域的MCBPs，我们将其视为MCBP家族的进化中间体。
