6SMT

S-enantioselective imine reductase from Mycobacterium smegmatis

6SMT の概要

• エントリーDOI: 10.2210/pdb6smt/pdb
• 分子名称: 6-phosphogluconate dehydrogenase, NAD-binding, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, FORMIC ACID, ... (8 entities in total)
• 機能のキーワード: oxidoreductase, imine reductase
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 160673.07

構造登録者

Meyer, T.,Zumbraegel, N.,Geerds, C.,Groeger, H.,Niemann, H.H. (登録日: 2019-08-22, 公開日: 2020-08-12, 最終更新日: 2024-01-24)

主引用文献

Meyer, T.,Zumbragel, N.,Geerds, C.,Groger, H.,Niemann, H.H.
Structural Characterization of an S -enantioselective Imine Reductase from Mycobacterium Smegmatis .
Biomolecules, 10:-, 2020

PubMed Abstract: NADPH-dependent imine reductases (IREDs) are enzymes capable of enantioselectively reducing imines to chiral secondary amines, which represent important building blocks in the chemical and pharmaceutical industry. Since their discovery in 2011, many previously unknown IREDs have been identified, biochemically and structurally characterized and categorized into families. However, the catalytic mechanism and guiding principles for substrate specificity and stereoselectivity remain disputed. Herein, we describe the crystal structure of -IRED- from together with its cofactor NADPH. -IRED- belongs to the -enantioselective superfamily 3 (SFam3) and is the first IRED from SFam3 to be structurally described. The data presented provide further evidence for the overall high degree of structural conservation between different IREDs of various superfamilies. We discuss the role of Asp170 in catalysis and the importance of hydrophobic amino acids in the active site for stereospecificity. Moreover, a separate entrance to the active site, potentially functioning according to a gatekeeping mechanism regulating access and, therefore, substrate specificity is described.

PubMed: 32751900
DOI: 10.3390/biom10081130

実験手法

X-RAY DIFFRACTION (1.55 Å)