ArticleBiomolecules2021
A Novel One-Pot Enzyme Cascade for the Biosynthesis of Cladribine Triphosphate.
Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A Modular Nucleoside Kinase Cascade for the Synthesis of Ribonucleoside Triphosphates.Biotechnology and bioengineering · 2026Article
- Substrate Specificity of B12-Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications.Chembiochem : a European journal of chemical biology · 2026Article
- Design, Synthesis, and Application of Immobilized Enzymes on Artificial Porous Materials.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Chemo-enzymatic production of base-modified ATP analogues for polyadenylation of RNA.Chemical science · 2024Article
- Magnetic Multi-Enzymatic System for Cladribine Manufacturing.International journal of molecular sciences · 2022Article
- Rational Design of a Thermostable 2'-Deoxyribosyltransferase for Nelarabine Production by Prediction of Disulfide Bond Engineering Sites.International journal of molecular sciences · 2022Article
- A Multi-enzyme Cascade for the Biosynthesis of AICA Ribonucleoside Di- and Triphosphate.Chembiochem : a European journal of chemical biology · 2022Article
- Make or break: the thermodynamic equilibrium of polyphosphate kinase-catalysed reactions.Beilstein journal of organic chemistry · 2022Article
- Cost-Effective Production of ATP and S-Adenosylmethionine Using Engineered Multidomain Scaffold Proteins.Biomolecules · 2021Article
- Biotechnological and Biomedical Applications of Enzymes Involved in the Synthesis of Nucleosides and Nucleotides.Biomolecules · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
Cladribine triphosphate is the active compound of the anti-cancer and multiple sclerosis drug Mavenclad (cladribine). Biosynthesis of such non-natural deoxyribonucleotides is challenging but important in order to study the pharmaceutical modes of action. In this study, we developed a novel one-pot enzyme cascade for the biosynthesis of cladribine triphosphate, starting with the nucleobase 2Cl-adenine and the generic co-substrate phosphoribosyl pyrophosphate. The cascade is comprised of the three enzymes, namely, adenine phosphoribosyltransferase (APT), polyphosphate kinase (PPK), and ribonucleotide reductase (RNR). APT catalyzes the binding of the nucleobase to the ribose moiety, followed by two consecutive phosphorylation reactions by PPK. The formed nucleoside triphosphate is reduced to the final product 2Cl-deoxyadenonsine triphosphate (cladribine triphosphate) by the RNR. The cascade is feasible, showing comparative product concentrations and yields to existing enzyme cascades for nucleotide biosynthesis. While this study is limited to the biosynthesis of cladribine triphosphate, the design of the cascade offers the potential to extend its application to other important deoxyribonucleotides.
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