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Stereoselectivity and Structural Characterization of an Imine Reductase (IRED) from Amycolatopsis orientalis

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† School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, United Kingdom
‡ York Structural Biology Laboratory, Department of Chemistry, University of York, YO10 5DD York, United Kingdom
*(G.G.) E-mail: [email protected]
*(N.J.T.) E-mail: [email protected]
Cite this: ACS Catal. 2016, 6, 6, 3880–3889
Publication Date (Web):May 10, 2016
https://doi.org/10.1021/acscatal.6b00782
Copyright © 2016 American Chemical Society
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    The imine reductase AoIRED from Amycolatopsis orientalis (Uniprot R4SNK4) catalyzes the NADPH-dependent reduction of a wide range of prochiral imines and iminium ions, predominantly with (S)-selectivity and with ee’s of up to >99%. AoIRED displays up to 100-fold greater catalytic efficiency for 2-methyl-1-pyrroline (2MPN) compared to other IREDs, such as the enzyme from Streptomyces sp. GF3546, which also exhibits (S)-selectivity, and thus, AoIRED is an interesting candidate for preparative synthesis. AoIRED exhibits unusual catalytic properties, with inversion of stereoselectivity observed between structurally similar substrates, and also, in the case of 1-methyl-3,4-dihydroisoquinoline, for the same substrate, dependent on the age of the enzyme after purification. The structure of AoIRED has been determined in an “open” apo-form, revealing a canonical dimeric IRED fold in which the active site is formed between the N- and C-terminal domains of participating monomers. Co-crystallization with NADPH gave a “closed” form in complex with the cofactor, in which a relative closure of domains, and associated loop movements, has resulted in a much smaller active site. A ternary complex was also obtained by cocrystallization with NADPH and 1-methyl-1,2,3,4-tetrahydroisoquinoline [(MTQ], and it reveals a binding site for the (R)-amine product, which places the chiral carbon within 4 Å of the putative location of the C4 atom of NADPH that delivers hydride to the C═N bond of the substrate. The ternary complex has permitted structure-informed mutation of the active site, resulting in mutants including Y179A, Y179F, and N241A, of altered activity and stereoselectivity.

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    • Synthesis of substrates and product standards; cloning, expression, and mutation protocols; details of analytical protocols including chiral HPLC and GC traces of products; X-ray crystallography data; pH and temperature optima studies; tables of mutant kinetic data (PDF)

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