Table 1.
Kinetic comparison of T. cruzi AdoMetDC and AdoMetDC/prozyme heterodimer. AdoMetDC and prozyme proteins were coexpressed in E. coli followed by copurification as described in Materials and Methods. Error is the standard error of the fit
| No putrescine | 5 mM putrescine | Fold change by putrescine | |||||||
|---|---|---|---|---|---|---|---|---|---|
| kcat (s-1) | Km (μM) | kcat/Km (M-1s-1) | kcat (s-1) | Km (μM) | kcat/Km (M-1s-1) | kcat | Km | kcat/Km | |
| A. T. cruzi AdoMetDC | |||||||||
| TcAdoMetDC | 0.005 ± 0.001 | 540 ± 350 | 9.3 ± 6.6 | 0.02 ± 0.003 | 130 ± 63 | 150 ± 76 | 4.0 | 0.24 | 17 |
| TcAdoMetDC/Tcprozyme | 0.60 ± 0.09 | 580 ± 200 | 1030 ± 400 | 0.84 ± 0.06 | 170 ± 42 | 5100±1900 | 1.4 | 0.29 | 4.9 |
| Fold change by prozyme | 120 | 1.1 | 110 | 41 | 1.3 | 32 | |||
| B. T. brucei AdoMetDC* | |||||||||
| TbAdoMetDC | 0.0013 | 0.38 | 3.4 | 0.0082 | 0.24 | 35 | 6.3 | 0.63 | 10 |
| TbAdoMetDC/Tbprozyme | 1.4 | 0.11 | 12,000 | 1.7 | 0.17 | 11,000 | 1.2 | 1.5 | 0.92 |
| Fold change by prozyme | 1100 | 0.3 | 3500 | 210 | 0.71 | 310 | |||
*
Data taken from [19]