6xu3
(R)-selective amine transaminase from Shinella sp.
Structural highlights
FunctionA0A4Q8MG35_9HYPH Acts on leucine, isoleucine and valine.[ARBA:ARBA00003109] Publication Abstract from PubMedAmine transaminases (ATAs) are used to synthesize enantiomerically pure amines, which are building blocks for pharmaceuticals and agrochemicals. (R) -selective ATAs belong to the fold type IV PLP dependent enzymes and different sequence-, structure- and substrate scope-based features have been identified in the past decade. However, our knowledge is still restricted due to the limited number of characterized (R) -ATAs with additional bias towards fungal origin. We aimed to expand the toolbox of (R) -ATAs and contribute to the understanding of this enzyme subfamily. We identified and characterized four new (R) -ATAs. The ATA from Exophiala sideris contains a motif characteristic for D-ATAs, which was previously believed to be a disqualifying factor for (R) -ATA activity. The crystal structure of the ATA from Shinella is the first from a gram-negative bacterium. The ATAs from Pseudonocardia acaciae and Tetrasphaera japonica are the first characterized (R) -ATAs with a shortened/missing N-terminal helix. The active site charges vary significantly between the new and known ATAs correlating with their diverging substrate scope. Expanding the Toolbox of (R)-selective Amine Transaminases by Identification and Characterization of new Members.,Telzerow A, Paris J, Hakansson M, Gonzalez-Sabin J, Rios-Lombardia N, Groger H, Moris F, Schurmann M, Schwab H, Steiner K Chembiochem. 2020 Nov 26. doi: 10.1002/cbic.202000692. PMID:33242357[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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