6XU3

(R)-selective amine transaminase from Shinella sp.

Summary for 6XU3

• Entry DOI: 10.2210/pdb6xu3/pdb
• Descriptor: Class IV aminotransferase, PYRIDOXAL-5'-PHOSPHATE, CHLORIDE ION, ... (9 entities in total)
• Functional Keywords: fold iv plp-dependent enzyme, amine transaminase, transferase
• Biological source: Shinella sp. JR1-6
• Total number of polymer chains: 4
• Total formula weight: 149192.82

Authors

Telzerow, A.,Hakansson, M.,Steiner, K. (deposition date: 2020-01-17, release date: 2020-12-09, Last modification date: 2024-01-24)

Primary citation

Telzerow, A.,Paris, J.,Hakansson, M.,Gonzalez-Sabin, J.,Rios-Lombardia, N.,Groger, H.,Moris, F.,Schurmann, M.,Schwab, H.,Steiner, K.
Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.
Chembiochem, 22:1232-1242, 2021

PubMed Abstract: Amine 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.

PubMed: 33242357
DOI: 10.1002/cbic.202000692

Experimental method

X-RAY DIFFRACTION (2.1 Å)