5ucw | pdb_00005ucw

Cytochrome P411 P-4 A82L A78V F263L amination catalyst

spinqualitylabelsall models 5ucw, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ucw is a 2 chain structure with sequence from Atcc 14581. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [F2Q7T0_BACME] Functions as a fatty acid monooxygenase.[PIRNR:PIRNR000209] Publication Abstract from PubMed C-H bonds are ubiquitous structural units of organic molecules. Although these bonds are generally considered to be chemically inert, the recent emergence of methods for C-H functionalization promises to transform the way synthetic chemistry is performed. The intermolecular amination of C-H bonds represents a particularly desirable and challenging transformation for which no efficient, highly selective, and renewable catalysts exist. Here we report the directed evolution of an iron-containing enzymatic catalyst-based on a cytochrome P450 monooxygenase-for the highly enantioselective intermolecular amination of benzylic C-H bonds. The biocatalyst is capable of up to 1,300 turnovers, exhibits excellent enantioselectivities, and provides access to valuable benzylic amines. Iron complexes are generally poor catalysts for C-H amination: in this catalyst, the enzyme's protein framework confers activity on an otherwise unreactive iron-haem cofactor. Enantioselective, intermolecular benzylic C-H amination catalysed by an engineered iron-haem enzyme.,Prier CK, Zhang RK, Buller AR, Brinkmann-Chen S, Arnold FH Nat Chem. 2017 Jul;9(7):629-634. doi: 10.1038/nchem.2783. Epub 2017 May 29. PMID:28644476 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 NADPH-Cytochrome P450 Reductase

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