5fr9 | pdb_00005fr9

Structure of transaminase ATA-117 arRmut11 from Arthrobacter sp. KNK168 inhibited with 1-(4-Bromophenyl)-2-fluoroethylamine

spinqualitylabelsall models 5fr9, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fr9 is a 12 chain structure with sequence from Arthrobacter sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.81Å Ligands: 9HC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F7J696_9MICC Publication Abstract from PubMed Transaminases are valuable enzymes for industrial biocatalysis and enable the preparation of optically pure amines. For these transformations they require either an amine donor (amination of ketones) or an amine acceptor (deamination of racemic amines). Herein transaminases are shown to react with aromatic beta-fluoroamines, thus leading to simultaneous enantioselective dehalogenation and deamination to form the corresponding acetophenone derivatives in the absence of an amine acceptor. A series of racemic beta-fluoroamines was resolved in a kinetic resolution by tandem hydrodefluorination/deamination, thus giving the corresponding amines with up to greater than 99 % ee. This protocol is the first example of exploiting the catalytic promiscuity of transaminases as a tool for novel transformations. Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.,Cuetos A, Garcia-Ramos M, Fischereder EM, Diaz-Rodriguez A, Grogan G, Gotor V, Kroutil W, Lavandera I Angew Chem Int Ed Engl. 2016 Feb;55(9):3144-7. doi: 10.1002/anie.201510554. Epub , 2016 Feb 2. PMID:26836037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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