Phosphorylation Catalyzed by Dihydroxyacetone Kinase

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...

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Bibliographic Details
Published inEuropean journal of organic chemistry Vol. 2018; no. 23; pp. 2892 - 2895
Main Authors Gauss, Dominik, Sánchez‐Moreno, Israel, Oroz‐Guinea, Isabel, García‐Junceda, Eduardo, Wohlgemuth, Roland
Format Journal Article
LanguageEnglish
Published Weinheim Wiley Subscription Services, Inc 22.06.2018
Subjects
Biocatalysis
Dihydroxyacetone
Enantiomers
Enzyme catalysis
Homogeneous catalysis
Kinases
Metabolites
NMR spectroscopy
Phosphorylation
Regeneration
Substrates
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Summary: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. Biocatalytic phosphorylations catalyzed by recombinant dihydroxyacetone kinase have been investigated with quantitative 31P NMR spectroscopy and pyruvate‐kinase‐catalyzed ATP regeneration starting with dihydroxyacetone as substrate. A nearly 100 % conversion of d‐glyceraldehyde to d‐glyceraldehyde 3‐phosphate has been found.
ISSN:1434-193X
1099-0690
DOI:10.1002/ejoc.201800350