5l86

engineered ascorbate peroxidise

spinqualitylabelsall models 5l86, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l86 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, SO4 NonStd Res: MHS Activity: L-ascorbate peroxidase, with EC number 1.11.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 Ndelta-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. A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme.,Green AP, Hayashi T, Mittl PR, Hilvert D J Am Chem Soc. 2016 Sep 7;138(35):11344-52. doi: 10.1021/jacs.6b07029. Epub 2016 , Aug 26. PMID:27500802 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ascorbate peroxidase

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