0428同步年報-2021-全

Life Science 043 capacity to the bulkier PET. PET has been present in our world for less than 70 years; which period is believed too short for microorganisms to generate PET decomposing enzymes de novo . Modifying existing enzymes to adapt the newly emerged substances would be a rapid and efficient strategy. For Ser/Ile DM, mutating as few as three nucleotides can result in His-to-Ser and Phe-to-Ile substitutions. In addition to the evolutionary significance, DM could be an important strategy to obtain more PET hydrolytic enzymes. Considering that the development of bio-based PET degradation platforms might require enzymes that match various vectors or operate under varied conditions, establishing a panel of PET hydrolytic enzymes should be necessary. In addition, these results highlight the importance of crystallography in studying enzyme mechanisms, as information, such as amino-acid side-chain wobbling and loop vibration, are difficult to access unless crystal structures are solved. Moreover, the two residues associated with DM that do not directly contact the substrate can influence the architecture of the substrate-binding pocket. These facts encourage us to expand the range of investigation when looking at the catalytic center, as the amino acids that are not directly involved in forming the active site might deploy critical effects to govern the enzyme actions (Reported by Rey-Ting Guo, Hubei University, China). This report features the works of Rey-Ting Guo and his collaborators published in Nat. Catal. 4 , 425 (2021), FEBS J. 285 , 3717 (2018) and Nat. Commun. 8 , 2106 (2017). The comparisons of enzyme-mediated degradation towards natural and synthetic macromolecules were also comprehensively summarized and published in Nat. Rev. Chem. 4 , 114 (2020) . TPS 05A Protein Microcrystallography TLS 15A1 IASW – Biopharmaceutical Protein Crystallography • Protein Crystallography • Biological Macromolecules, Protein Structures, Life Science References 1. R. Wei, W. Zimmermann, Microb. Biotechnol. 10 , 1308 (2017). 2. C. C. Chen, L. Dai, L. Ma, R. T. Guo, Nat. Rev. Chem. 4 , 114 (2020). 3. S. Yoshida, K. Hiraga, T. Takehana, I. Taniguchi, H. Yamaji, Y. Maeda, K. Toyohara, K. Miyamoto, Y. Kimura, K. Oda, Science 351 , 1196 (2016). 4. X. Han, W. Liu, J. W. Huang, J. Ma, Y. Zheng, T. P. Ko, L. Xu, Y. S. Cheng, C. C. Chen, R. T. Guo, Nat. Commun. 8 , 2106 (2017). 5. C. C. Chen, X. Han, T. P. Ko, W. Liu, R. T. Guo, FEBS J. 285 , 3717 (2018). 6. C. C. Chen, X. Han, X. Li, P. Jiang, D. Niu, L. Ma, W. Liu, S. Li, Y. Qu, H. Hu, J. Min, Y. Yang, L. Zhang, W. Zeng, J. W. Huang, L. Dai, R. T. Guo, Nat. Catal. 4 , 425 (2021).