5L86
engineered ascorbate peroxidise
Summary for 5L86
| Entry DOI | 10.2210/pdb5l86/pdb |
| Descriptor | Ascorbate peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | protein engineering, peroxidase, heme, apx2, methyl histidine, oxidoreductase |
| Biological source | Glycine max (Soybean) |
| Total number of polymer chains | 2 |
| Total formula weight | 55437.82 |
| Authors | Hayashi, T.,Mittl, P.,Hilvert, D. (deposition date: 2016-06-07, release date: 2017-03-01, Last modification date: 2024-01-10) |
| Primary citation | Green, A.P.,Hayashi, T.,Mittl, P.R.,Hilvert, D. A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme. J. Am. Chem. Soc., 138:11344-11352, 2016 Cited by PubMed Abstract: Enzymes rely on complex interactions between precisely positioned active site residues as a mechanism to compensate for the limited functionality contained within the genetic code. Heme enzymes provide a striking example of this complexity, whereby the electronic properties of reactive ferryl intermediates are finely tuned through hydrogen bonding interactions between proximal ligands and neighboring amino acids. Here, we show that introduction of a chemically programmed proximal Nδ-methyl histidine (NMH) ligand into an engineered ascorbate peroxidase (APX2) overcomes the reliance on the conserved Asp-His hydrogen bonding interaction, leading to a catalytically modified enzyme (APX2 NMH), which is able to achieve a significantly higher number of turnovers compared with APX2 without compromising catalytic efficiency. Structural, spectroscopic and kinetic characterization of APX2 NMH and several active site variants provides valuable insights into the role of the Asp-His-Fe triad of heme peroxidases. More significantly, simplification of catalytic mechanisms through the incorporation of chemically optimized ligands may facilitate efforts to create and evolve new active site heme environments within proteins. PubMed: 27500802DOI: 10.1021/jacs.6b07029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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