New perspective on zinc biochemistry: cocatalytic sites in multi-zinc enzymes.
New perspective on zinc biochemistry: cocatalytic sites in multi-zinc enzymes.
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DOI：
10.1021/bi00077a001
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发表时间：
1993-07
期刊：
影响因子：
2.9
通讯作者：
B. Vallée;D. Auld
中科院分区：
文献类型：
--
作者：
B. Vallée;D. Auld
锌是一个不可分割的组成部分，大量和各种蛋白质参与了多种生命过程，占其在新陈代谢，遗传信息的传递，生长和发育的必要性。锌的化学稳定性，但立体化学灵活，无毒的性质结合其两性性质是一系列锌结合基序的生物化学组织的基础，这些基序对生命及其延续至关重要。我们对生物学中锌结合位点的第一个观点集中在锌的协调、功能和单锌酶的结构以及锌在基因表达控制中的现有有限知识（Vallee & Auld，1990a）。从那时起，对含有两个或多个锌原子的锌酶进行了系统的研究，并在锌酶中定义了一个新的锌结合基序，即共催化或共活性位点。目前的观点集中在这组多锌酶的性质。
Zinc is an integral component of a large number and variety of proteins involved in a multiplicity of vital processes accounting for its essentiality in metabolism, transmission of the geneticmessage, growth, and development. The chem-ically stable but stereochemically flexible, nontoxic nature of zinc combined with its amphoteric properties is the basis for the biochemical organization of a series of zinc binding motifs critical to life and its perpetuation. Our first perspective on zinc binding sites in biology focused on the zinc coordination, function, and structure of mono-zincenzymes and the existing limited knowledge of zinc in the control of gene expression (Vallee & Auld, 1990a). Since that time systematic exam-ination of zinc enzymes containing two or more zinc atoms has become available and has led to the definition of a new zinc binding motif in zinc enzymes, the cocatalytic or coactive site. The present perspective focuses on the properties of this group of multi-zinc enzymes.