Birhanu Mekuaninte Kinfu
University of Hamburg, Germany
Title: Biocatalytic asymmetric phosphorylation catalyzed by recombinant glycerate-2-kinase
Biography
Biography: Birhanu Mekuaninte Kinfu
Abstract
D-Glycerate-2-phosphate is an important substrate and crucial metabolite of central carbon metabolism, glycolysis/ gluconeogenesis and pentose phosphate pathway, glycine, serine and threonine metabolism, methane metabolism, biosynthesis of plant secondary metabolites, phenylpropanoids, terpenoids and steroids, alkaloids derived from shikimate pathway, antibiotics, amino acids. Therefore an efficient, robust and scalable route for the preparation of enantio pure D-glycerate-2-phosphate is needed. A straightforward one-step biocatalytic phosphorylation of glyceric acid catalyzed by a recombinant glycerate 2-kinase heterologously expressed as maltose binding protein fusion has been investigated using racemic and the enantiopure D- and L-glycerate as substrate. The reaction was coupled with the phosphoenolpyruvate/ pyruvate-kinase-system for ATP-regeneration and monitored by 31P-NMR spectroscopy. This phosphorylation reaction using recombinant glycerate 2-kinase is highly enantio-selective and sustainable, as it yields enantiomerically pure D-Glycerate-2-phosphate in less reaction steps and with higher purity than chemical routes.