Department of Environmental Science and Bioscience, Kristianstad University, 29188 Kristianstad, Sweden.
Department of Biochemistry and Structural Biology, Lund University, 22100 Lund, Sweden.
Molecules. 2020 Sep 25;25(19):4405. doi: 10.3390/molecules25194405.
Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to alteration of the original function of the protein. However, if the function is preserved interesting biotechnological applications can be developed. This review will cover the knowledge about the interaction between hCAs and nanomaterials. We will highlight how the interaction may lead to conformational changes that render the enzyme inactive. Moreover, the importance of different factors on the final effect on hCAs, such as protein stability, protein hydrophobic or charged patches and chemistry of the nanoparticle surface will be discussed.
人碳酸酐酶（hCA）属于一类具有良好特征的金属酶，可催化二氧化碳转化为碳酸氢盐。目前已知有 15 种不同功能和分布在体内的人碳酸酐酶同工酶。这与人碳酸酐酶变体与几种疾病（如青光眼、癫痫、高山病、溃疡、骨质疏松症、肥胖症和癌症）的相关性有关。这篇综述将重点介绍两种人同工酶，即 hCA I 和 hCA II。它们都是细胞溶质酶，具有相似的拓扑结构和 60%的序列同源性，但催化效率和稳定性不同。一般来说，蛋白质会在表面上吸附，hCA I 和 hCA II 也是如此。吸附过程可能导致蛋白质原始功能的改变。然而，如果功能得以保留，就可以开发出有趣的生物技术应用。这篇综述将涵盖关于 hCA 与纳米材料相互作用的知识。我们将重点介绍这种相互作用如何导致构象变化，使酶失活。此外，还将讨论不同因素对 hCA 的最终影响的重要性，如蛋白质稳定性、蛋白质疏水区或带电区以及纳米粒子表面的化学性质。
