Whittaker James W
Department of Biochemistry and Molecular Biology, OGI School of Science and Engineering, OHSU, Beaverton, Oregon 97006, USA.
Adv Protein Chem. 2002;60:1-49. doi: 10.1016/s0065-3233(02)60050-6.
The free radical-coupled copper catalytic motif has emerged as the unifying feature of a new family of enzymes, the radical copper oxidases. Their highly evolved active sites include a novel amino acid modification, the Tyr-Cys dimer, that forms spontaneously through self-processing of the protein during its maturation. The active site is remarkable in the extent to which metal ligands participate in the catalytic process. Rather than simply coordinating the metal ion, the ligands perform essential redox and proton-transfer functions in the chemistry of the active site, directed by their interactions with the copper center in the protein. The wide phylogenetic distribution and range of functions represented within the family hint of a fundamental role for these enzymes in the biology of oxygen. The roles for these enzymes are further expanding through a variety of biotechnological applications.
自由基偶联铜催化基序已成为一类新酶——自由基铜氧化酶家族的统一特征。它们高度进化的活性位点包括一种新型氨基酸修饰，即酪氨酸 - 半胱氨酸二聚体，其在蛋白质成熟过程中通过自身加工自发形成。活性位点在金属配体参与催化过程的程度方面非常显著。这些配体并非简单地配位金属离子，而是在活性位点的化学反应中执行重要的氧化还原和质子转移功能，这是由它们与蛋白质中铜中心的相互作用所引导的。该家族内广泛的系统发育分布和功能范围暗示了这些酶在氧生物学中的基础作用。通过各种生物技术应用，这些酶的作用正在进一步扩展。
