Impact Factor 3.644 | CiteScore 3.2
More on impact ›

Correction ARTICLE

Front. Bioeng. Biotechnol., 26 October 2020 | https://doi.org/10.3389/fbioe.2020.606584

Corrigendum: Modular Enzymatic Cascade Synthesis of Nucleotides Using a (d)ATP Regeneration System

Maryke Fehlau1,2, Felix Kaspar1,2, Katja F. Hellendahl1, Julia Schollmeyer1,2, Peter Neubauer1 and Anke Wagner1,2*
  • 1Chair of Bioprocess Engineering, Institute of Biotechnology, Faculty III Process Sciences, Technische Universität Berlin, Berlin, Germany
  • 2BioNukleo GmbH, Berlin, Germany

A Corrigendum on
Modular Enzymatic Cascade Synthesis of Nucleotides Using a (d)ATP Regeneration System

by Fehlau, M., Kaspar, F., Hellendahl, K. F., Schollmeyer, J., Neubauer, P., and Wagner, A. (2020). Front. Bioeng. Biotechnol. 8:854. doi: 10.3389/fbioe.2020.00854

In the original article, there was an error. We did not receive the expression plasmid of DmdNK from Daniela Ubiali (which is written 2x in the manuscript), but from Prof. Munch-Petersen.

A correction has been made to Materials and Methods, General Information, paragraph 3.

The corrected paragraph appears below:

“Wild-type nucleoside and nucleotide kinases were obtained from BioNukleo GmbH (Berlin, Germany) except for wide-spectrum deoxynucleoside kinase from Drosophila melanogaster (DmdNK). The expression vector of DmdNK was kindly provided by Prof. Birgitte Munch-Petersen (Roskilde University). According to the manufacturer the kinases possess the following substrate specificities: adenosine kinase (AK, NK14), guanylate kinase (GMPK, NMPK21) and adenylate kinase (AMPK, NMPK23) convert purine nucleoside/nucleotide substrates, while uridine monophosphate-cytidine monophosphate kinase (UMP-CMPK, NMPK22) and nucleoside diphosphate kinase (NDPK, NDPK32) accept both purine and pyrimidine nucleoside/nucleotide substrates. All enzymes obtained from BioNukleo were provided as stock solutions (0.1 to 1 mg/mL) and aliquots stored at −20°C until use. Pyruvate kinase (PK, P9136) was obtained from Sigma Aldrich as lyophilized powder, dissolved in 70 mM Tris–HCl pH 7.6 (1.74 mg/mL) and stored in aliquots at −20°C. All enzymes are active at 37°C and combinable in the same reaction buffer (70 mM Tris–HCl pH 7.6, 5 mM MgCl2).”

A correction has been made to Acknowledgments.

The corrected paragraph appears below:

“We thank Prof. Munch-Petersen for supplying Drosophila melanogaster deoxynucleoside kinase plasmid (DmdNK). We thank the Open Access Publishing funds of TU Berlin for the support of this publication.”

The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.

Keywords: enzymatic cascade synthesis, nucleoside-5′-triphosphate, one-pot multi-enzyme reaction, nucleotide analog, nucleotide kinase, nucleoside kinase, modular, ATP regeneration system

Citation: Fehlau M, Kaspar F, Hellendahl KF, Schollmeyer J, Neubauer P and Wagner A (2020) Corrigendum: Modular Enzymatic Cascade Synthesis of Nucleotides Using a (d)ATP Regeneration System. Front. Bioeng. Biotechnol. 8:606584. doi: 10.3389/fbioe.2020.606584

Received: 15 September 2020; Accepted: 22 September 2020;
Published: 26 October 2020.

Approved by:

Frontiers Editorial Office, Frontiers Media SA, Switzerland

Copyright © 2020 Fehlau, Kaspar, Hellendahl, Schollmeyer, Neubauer and Wagner. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Anke Wagner, anke.wagner@tu-berlin.de