| 초록 |
Glycerol dehydratase (GDHt) is a rate-limiting enzyme which converts glycerol into 3-hydroxypropanal (3-HPA) and subsequently transformed into 1,3-propandiol or 3-hydroxypropionic acid. However, GDHt undergoes a mechanism-based inactivation due to the accumulation of an inactive cofactor (B12). The prolonged stability and slower inactivation of the enzyme could be attributed to the terminal residues stabilization of the fused subunits, which distantly influences the Co-N bond between cobalt and dimethylbenzimidazole moiety of B12. Overall, our findings provide novel insights into linker-based enzymatic modulation of GDHt and propose a feasible approach for improving the activity of GDHt in glycerol bioconversion at industrial level. |
