| 초록 |
Phosphomannose isomerase (PMI) catalyzes reversible conversion between fructose 6-phosphate and mannose 6-phosphate. In spite of the wide applicability, its reaction characteristics is not attractive because its equilibrium usually lies close to substrate, fructose 6-phosphate. However, PMI from Corynebacterium glutamicum ATCC13032 had reaction equilibrium close to product. PMIs use zinc ion as cofactor. Therefore, when PMI is incubated with EDTA, they usually lose their activity. However, PMI from C. glutamicum ATCC13032 constantly showed unchanged activity in spite of the incubation with 10 mM EDTA. Additionally, to increase the production of mannose 6-phosphate, we tried enzyme evolution based on smart library construction. Saturation mutagenesis were performed to four active site residues based on smart library construction method. These unveiled characteristics of PMI from C. glutamicum ATCC13032 would be useful in the biological production of high value-added compounds. |
