5FR9

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

Summary for 5FR9

• Entry DOI: 10.2210/pdb5fr9/pdb
• Descriptor: (R)-AMINE TRANSAMINASE, [4-[3-(4-bromophenyl)-3-oxidanylidene-propyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl phosphate (3 entities in total)
• Functional Keywords: transferase, transminase, aminotransferase, plp, inhibitor, fluoroamine
• Biological source: ARTHROBACTER SP.
• Total number of polymer chains: 12
• Total formula weight: 447990.83

Authors

Cuetos, A.,Kroutil, W.,Lavandera, I.,Grogan, G. (deposition date: 2015-12-16, release date: 2016-03-02, Last modification date: 2024-11-06)

Primary citation

Cuetos, A.,Garcia-Ramos, M.,Fischereder, E.,Diaz-Rodriguez, A.,Grogan, G.,Gotor, V.,Kroutil, W.,Lavandera, I.
Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched Beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.
Angew.Chem.Int.Ed.Engl., 55:3144-, 2016

PubMed Abstract: 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 β-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 β-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.

PubMed: 26836037
DOI: 10.1002/ANIE.201510554

Experimental method

X-RAY DIFFRACTION (2.81 Å)