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Characterization of glycerol dehydratase expressed by fusing its α- and β-subunits



The gdh and gdhr genes, encoding B 12 -dependent glycerol dehydratase (GDH) and glycerol dehydratase reactivase (GDHR), respectively, in Klebsiella pneumoniae, were cloned and expressed in E. coli . Part of the β-subunit was lost during GDH purification when co-expressing α, β and γ subunit. This was overcome by fusing the β-subunit to α- or γ-subunit with/without the insertion of a linker peptide between the fusion moieties. The kinetic properties of the fusion enzymes were characterized and compared with wild type enzyme. The results demonstrated that the fusion protein GDHALB/C, constructed by linking the N -terminal of β-subunit to the C -terminal of α subunit through a (Gly 4 Ser) 4 linker peptide, had the greatest catalytic activity. Similar to the wild-type enzyme, GDHALB/C underwent mechanism-based inactivation by glycerol during catalysis and could be reactivated by GDHR.



Biotechnology LettersSpringer Journals

Published: May 1, 2009

DOI: 10.1007/s10529-009-9911-x

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