Correction: A high-throughput dual system to screen polyphosphate kinase mutants for efficient ATP regeneration in l-theanine biocatalysis
Biotechnology for Biofuels and Bioproducts volume 16, Article number: 138 (2023)
Correction: Biotechnology for Biofuels and Bioproducts (2023) 16:122 https://doi.org/10.1186/s13068-023-02361-9
Following publication of the original article , it came to the attention of the authors that the sequence of PPK12 was previously reported in an earlier publication  and registered under the UniProt ID: A0A3D5XRJ5. The sequence of EbPPK from this manuscript was registered under the Genbank ID: HCY06753.1. The protein sequence is of the same strain origin (Erysipelotrichaceae bacterium). However, ChPPK is the focus of research in this article and not EbPPK. The authors apologize for not being aware of the previous publication and have now cited the previous publication reporting the sequence  in the article. They have also cited  in the Results and Discussion section in relation to the fact that that EbPPK is better than ChPPK at regenerating ATP from AMP, which was reported by  previously.
The authors also state that the correction does not affect the discussion or conclusions and that they sincerely apologize for the unintentional errors.
The original article has been corrected.
Gao H, Li M, Wang Q, Liu T, Zhang X, Yang T, Xu M, Rao Z. A high-throughput dual system to screen polyphosphate kinase mutants for efficient ATP regeneration in l-theanine biocatalysis. Biotechnol Biofuels. 2023;16:122.
Tavanti M, Hosford J, Lloyd RC, Brown MJB. ATP regeneration by a single polyphosphate kinase powers multigram-scale aldehyde synthesisin vitro. Green Chem. 2021;23(2):828–37. https://doi.org/10.1039/D0GC03830J.
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Gao, H., Li, M., Wang, Q. et al. Correction: A high-throughput dual system to screen polyphosphate kinase mutants for efficient ATP regeneration in l-theanine biocatalysis. Biotechnol Biofuels 16, 138 (2023). https://doi.org/10.1186/s13068-023-02390-4