6AH7
D45W/H226G mutant of marine bacterial prolidase
Summary for 6AH7
| Entry DOI | 10.2210/pdb6ah7/pdb |
| Descriptor | Xaa-Pro dipeptidase, MANGANESE (II) ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | paraoxonase, hydrolase |
| Biological source | Pseudoalteromonas lipolytica |
| Total number of polymer chains | 4 |
| Total formula weight | 207075.21 |
| Authors | Jian, Y.,Yunzhu, X.,Lijuan, L. (deposition date: 2018-08-17, release date: 2019-09-18, Last modification date: 2023-11-22) |
| Primary citation | Yang, J.,Xiao, Y.Z.,Li, R.,Liu, Y.,Long, L.J. Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity. Biotechnol.Bioeng., 117:2694-2702, 2020 Cited by PubMed Abstract: Enzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions. PubMed: 32515491DOI: 10.1002/bit.27455 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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