22PE
Ethylene Forming Enzyme in complex with 2-oxoglutarate
Summary for 22PE
| Entry DOI | 10.2210/pdb22pe/pdb |
| Descriptor | 2-oxoglutarate-dependent ethylene/succinate-forming enzyme, 2-OXOGLUTARIC ACID, FE (II) ION, ... (4 entities in total) |
| Functional Keywords | complex, ethylene forming enzyme, oxidoreductase |
| Biological source | Pseudomonas savastanoi pv. phaseolicola |
| Total number of polymer chains | 1 |
| Total formula weight | 39606.41 |
| Authors | |
| Primary citation | Wang, M.,Shen, Z.,Wu, L.,Huang, W.,Zhou, J.,Gu, Y. Structure-guided surface engineering to improve the catalytic activity of ethylene-forming enzyme. Eng Microbiol, 6:100276-100276, 2026 Cited by PubMed Abstract: The ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate-dependent oxygenase superfamily, which can oxidize 2-oxoglutarate to form ethylene in an arginine-dependent reaction. While significant enzyme engineering efforts have targeted the active site and surface of EFE, to date, no variant with substantially improved activity has been reported. To enhance catalytic activity and broaden the application potential of EFE, this study developed a surface engineering strategy based on structural analysis and potentially new l-Arg binding information. The resulting variant, E213T, exhibited a 1.5-fold increase in catalytic activity and a 2.4-fold elevation in . Molecular dynamics simulations further revealed that this amino acid substitution reduced the affinity of the surface l-Arg binding site and altered the accessibility of ligands to the catalytic center. Our study provides a new perspective on the distal sites and functional relationships in protein engineering of EFE. PubMed: 42238545DOI: 10.1016/j.engmic.2026.100276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
No wwPDB Validation report is currently available for this entry.
