Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate-2-Kinase
| Autor: | Markus Obkircher, Bernhard Schoenenberger, Birhanu M. Kinfu, Norman Hardt, Wolfgang R. Streit, Roland Wohlgemuth, Jennifer Chow |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Glyceric acid Magnetic Resonance Spectroscopy Stereochemistry Recombinant Fusion Proteins 030106 microbiology Biology medicine.disease_cause Glyceric Acids Biochemistry Maltose-Binding Proteins law.invention 03 medical and health sciences chemistry.chemical_compound law Endopeptidases medicine Escherichia coli Thermotoga maritima Phosphorylation Molecular Biology chemistry.chemical_classification Kinase Organic Chemistry Substrate (chemistry) Stereoisomerism biology.organism_classification Kinetics Phosphotransferases (Alcohol Group Acceptor) 030104 developmental biology Enzyme chemistry Recombinant DNA Biocatalysis bacteria Molecular Medicine Phosphorus Radioisotopes |
| Zdroj: | Chembiochem : a European journal of chemical biology. 18(15) |
| ISSN: | 1439-7633 |
| Popis: | The efficient synthesis of pure d-glycerate-2-phosphate is of great interest due to its importance as an enzyme substrate and metabolite. Therefore, we investigated a straightforward one-step biocatalytic phosphorylation of glyceric acid. Glycerate-2-kinase from Thermotoga maritima was expressed in Escherichia coli, allowing easy purification. The selective glycerate-2-kinase-catalyzed phosphorylation was followed by 31 P NMR and showed excellent enantioselectivity towards phosphorylation of the d-enantiomer of glyceric acid. This straightforward phosphorylation reaction and subsequent product isolation enabled the preparation of enantiomerically pure d-glycerate 2-phosphate. This phosphorylation reaction, using recombinant glycerate-2-kinase, yielded d-glycerate 2-phosphate in fewer reaction steps and with higher purity than chemical routes. |
| Databáze: | OpenAIRE |
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