| 초록 |
The production of biodiesel has become an important strategy to address the fading petroleum reservoirs and environmental issues. Recently biological processes to produce high-value products from glycerol have drawn much attention. The first step of such processes is the dehydration from glycerol to form 3-hydroxypropanal (3-HPA), which can be catalyzed by glycerol dehydratase (GDHt). During the purification of KpGDHt, β subunit was highly prone to dissociate from the functional (αβγ)2 complex. This has been circumvented through the addition of a linker to fuse the α and β subunits to simplify the purification. Interestingly, the catalytic activity of the linked enzyme was improved than the unfused wild type. The structure, dynamics and kinetics advantages of this arrangement in fused proteins are not known. Therefore, it is of interest to probe into the structure and dynamics properties of the fused and unfused structures of KpGDHt using molecular dynamics simulation. |
