Exploring the biocatalytic potential of wild-type split transketolases
5 affiliations
- 1aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.
- 2bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.
- 3aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.
- 4bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.cManufacturing Futures Laboratory, University College London, 7 Sidings Street, London, E20 2AE, UK.
- 5aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.cManufacturing Futures Laboratory, University College London, 7 Sidings Street, London, E20 2AE, UK.
Abstract
Split transketolases (split TKs) are an underexplored class of carboligases with potential for application in biocatalysis. Here, we investigate ten split TKs and reveal substantial functional heterogeneity, with marked differences in substrate scope, activity, enantioselectivity, and robustness. The enzymes accepted diverse acceptors, aliphatic and aromatic, while retaining the canonical (S)-selectivity of full-length TKs. Pyruvate acceptance further revealed distinct catalytic behaviours, including cross-coupling and self-coupling specificity. Selected enzymes also displayed high organic solvent tolerance. Notably, pQR2829 combined high activity, strong stereocontrol, and cross-coupling specificity, whereas pQR2809 showed exceptional robustness and broad substrate acceptance. Overall, these findings establish split TKs as a diverse and promising class of carboligases for further biocatalytic development and engineering.
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BibTeX
@article{tonoli2026exploring,
title = {{Exploring the biocatalytic potential of wild-type split transketolases}},
author = {Alessia Tonoli and Silvia Anselmi and Yeke Ni and John M. Ward and Helen C. Hailes and Jack W. E. Jeffries},
journal = {RSC chemical biology},
year = {2026},
month = oct,
doi = {10.1039/d6cb00243a},
url = {https://europepmc.org/article/PMC/PMC13663882},
note = {CC BY},
}
RIS
TY - JOUR
TI - Exploring the biocatalytic potential of wild-type split transketolases
AU - Alessia Tonoli
AU - Silvia Anselmi
AU - Yeke Ni
AU - John M. Ward
AU - Helen C. Hailes
AU - Jack W. E. Jeffries
PY - 2026
DA - 2026/10/01
JO - RSC chemical biology
DO - 10.1039/d6cb00243a
UR - https://europepmc.org/article/PMC/PMC13663882
AB - Split transketolases (split TKs) are an underexplored class of carboligases with potential for application in biocatalysis. Here, we investigate ten split TKs and reveal substantial functional heterogeneity, with marked differences in substrate scope, activity, enantioselectivity, and robustness. The enzymes accepted diverse acceptors, aliphatic and aromatic, while retaining the canonical (S)-selectivity of full-length TKs. Pyruvate acceptance further revealed distinct catalytic behaviours, including cross-coupling and self-coupling specificity. Selected enzymes also displayed high organic solvent tolerance. Notably, pQR2829 combined high activity, strong stereocontrol, and cross-coupling specificity, whereas pQR2809 showed exceptional robustness and broad substrate acceptance. Overall, these findings establish split TKs as a diverse and promising class of carboligases for further biocatalytic development and engineering.
SN - 2633-0679
ER -