6SNL

(R)-selective amine transaminase from Exophiala sideris

6SNL の概要

• エントリーDOI: 10.2210/pdb6snl/pdb
• 分子名称: amine transaminase, PYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: fold iv plp-dependent enzyme, amine transaminase, transferase
• 由来する生物種: Exophiala sideris
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 233824.30

構造登録者

Telzerow, A.,Hakansson, M.,Steiner, K. (登録日: 2019-08-26, 公開日: 2020-12-09, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.129 Å)