Characterization of a Mannose-6-Phosphate Isomerase from Thermus thermophilus and Increased L-Ribose Production by Its R142N Mutant -- Yeom et al. 77 (3): 762 Data Supplement - Supplemental material -- Applied and Environmental Microbiology

Characterization of a Mannose-6-Phosphate Isomerase from Thermus thermophilus and Increased L-Ribose Production by Its R142N Mutant
Appl. Environ. Microbiol. Yeom et al. 77: 762

Supplemental material

Files in this Data Supplement:

Supplemental file 1 - SDS-PAGE analysis of the wild-type and alanine-substituted mutant enzymes in the active site of mannose-6-phosphate isomerases from T. thermophilus (Fig. S1); SDS-PAGE analysis of the wild-type and mutant enzymes at position 142 of mannose-6-phosphate isomerase from T. thermophilus (Fig. S2); determination of molecular mass of mannose-6-phosphate isomerase from T. thermophilus by gel-filtration chromatography (Fig. S3); effects of the Cu²⁺ concentration (Fig. S4), pH (Fig. S5) and temperature (Fig. S6) on the activity of T. thermophilus mannose-6-phosphate isomerase; time courses of L-ribose production from L-ribulose by the wild-type and R142N mutant mannose-6-phosphate isomerases from T. thermophilus (Fig. S7); effect of enzyme activity on L-ribose production by R142N mutant mannose-6-phosphate isomerase from T. thermophilus (Fig. S8); effect of substrate concentration on production and conversion yield of L-ribose by R142N mutant mannose-6-phosphate isomerase from T. thermophilus (Fig. S9).
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