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Título: | Phosphorylation Catalyzed by Dihydroxyacetone Kinase |
Autor: | Gauss, D.; Sánchez-Moreno, Israel CSIC ; Oroz-Guinea, I.; García-Junceda, Eduardo CSIC ORCID ; Wohlgemuth, Roland | Palabras clave: | Biocatalysis Enzyme catalysis Homogeneous catalysis Kinases Phosphorylation |
Fecha de publicación: | 22-jun-2018 | Editor: | Wiley-VCH | Citación: | European Journal of Organic Chemistry 2018(23): 2892-2895 (2018) | Resumen: | Site- and enantioselective kinases have been very useful catalysts for biocatalytic phosphorylations in straightforward syntheses of phosphorylated metabolites. Biocatalytic phosphorylations catalyzed by recombinant dihydroxyacetone kinase beyond the dihydroxyacetone substrate have been investigated with quantitative 31P NMR spectroscopy using pyruvate-kinase-catalyzed ATP regeneration. A nearly 100 % conversion of d-glyceraldehyde to d-glyceraldehyde 3-phosphate has been found. Interestingly, with pure l-glyceraldehyde as substrate, practically no formation of l-glyceraldehyde 3-phosphate was observed. | Versión del editor: | https://onlinelibrary.wiley.com/doi/full/10.1002/ejoc.201800350 | URI: | http://hdl.handle.net/10261/179399 | DOI: | 10.1002/ejoc.201800350 | ISSN: | 1434-193X |
Aparece en las colecciones: | (IQOG) Artículos |
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Fichero | Descripción | Tamaño | Formato | |
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Eur. J. Org. Chem. 10.1002ejoc.201800350_accepted.pdf | Artículo principal | 1,29 MB | Adobe PDF | Visualizar/Abrir |
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