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handle: 10261/179399
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.
Biocatalysis, Enzyme catalysis, Kinases, Phosphorylation, Homogeneous catalysis
Biocatalysis, Enzyme catalysis, Kinases, Phosphorylation, Homogeneous catalysis
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 16 | |
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
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