Improved stereocontrol in reductive aminases through steric modification of residues around substrate and cofactor binding pockets

Multiple residues have been identified at the cofactor and substrate binding pockets in a reductive aminase that can be exploited for stereocontrol through steric modification of their side chains.

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Publication Details

Journal
Catalysis Science & Technology
Published
2025-01-01
DOI
https://doi.org/10.1039/d5cy00308c
Citations
2
Primary Topic
Chemical Synthesis and Analysis
Type
article
Field-Weighted Citation Impact
1.61

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article

Improved stereocontrol in reductive aminases through steric modification of residues around substrate and cofactor binding pockets

Ruth T. Bradshaw Allen, Mario Prejanò, Godwin A. Aleku, Z.‐M. XIE et al.
2 citations
Catalysis Science & Technology
Chemical Synthesis and Analysis
1.61
article

Improved stereocontrol in reductive aminases through steric modification of residues around substrate and cofactor binding pockets

Ruth T. Bradshaw Allen, Mario Prejanò, Godwin A. Aleku, Z.‐M. XIE, Jake Gooderham, David D. Aleku, Julie Vignot, Beatrice-Maria Zabavaa
article en
2 citations

Abstract

Multiple residues have been identified at the cofactor and substrate binding pockets in a reductive aminase that can be exploited for stereocontrol through steric modification of their side chains.

Catalysis Science & TechnologyVol. 15(10)
King's College London (GB), University of Calabria (IT)
Leverhulme Trust, King's College London, Università della Calabria
Openalex Percentile: Top 18%
Chemical Synthesis and Analysis
1.61
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Improved stereocontrol in reductive aminases through steric modification of residues around substrate and cofactor binding pockets — Ruth T. Bradshaw Allen, Mario Prejanò, et al. · Catalysis Science & Technology (2025) | TGRS Research Map | TGRS