TABLE 1.
Substrate specificity of the carbohydrate kinase activity of Ydr109c and FGGY
The kinase activities of the recombinant purified His-Ydr109c and His-FGGY proteins were measured spectrophotometrically using the PK/LDH assay with 19 different sugars or sugar derivatives (all at a concentration of 1 mm). Enzymatic activities were corrected by control assays run in the absence of carbohydrate substrate. The results shown are mean relative activities ± S.D. resulting from three replicative measurements. ND, not detected; S.D., standard deviation.
| Substrate | FGGY activity | Ydr109c activity |
|---|---|---|
| % | % | |
| d-Ribulose | 100 ± 2 | 100 ± 3 |
| l-Ribulose | 8 ± 1 | ND |
| Ribitol | 21 ± 1 | ND |
| d-Xylulose | 1 ± 0.3 | ND |
| l-Xylulose | 1 ± 0.3 | ND |
| d-Glucose | ND | ND |
| Arabitol | ND | ND |
| Erythritol | ND | ND |
| l-Arabinose | ND | ND |
| d-Arabinose | ND | ND |
| d-Ribose | 1 ± 0.3 | ND |
| Glycerol | ND | ND |
| d-Ribulose 5-phosphate | ND | ND |
| Gluconate | ND | ND |
| 2-Deoxy-d-ribose | ND | ND |
| d-Lyxose | ND | ND |
| d-Ribose 5-phosphate | ND | ND |
| d-Mannitol | ND | ND |
| d-Ribose 1-phosphate | ND | ND |