Category:MichSt14A 34

Figure 3 shows the differing growth rate of wild-type and OmpF mutants when grown on maltotriose and maltooligosaccharides. The N-terminal mutations allow for growth on carbon sources larger than the normal exclusion limit.

Figure 8C shows the effect of point mutations on the activity of the inositol-3-phosphate synthase. The assay measured the inorganic phosphate liberated from glucose 6-phosphate which is dependent on the activity of the synthase enzyme.

Table 2 presents the partial alignment of conserved residues between Escherichia coli glycogen synthase and other bacterial glycogen syntheses and plant starch syntheses.

Table 5 shows sequence point mutations, deletions or truncations that result in glycogen storage disease type IV, caused by lethal or retarded function of glycogen branching enzyme.

Figure 2 shows sequence and structural homology to other defined aldo-keto reductases, notably human aldo-keto reductase AKR1C2.