Table 2.
Substrate | kcat (s−1) | Km (mM) | kcat/Km (M−1 s−1) |
---|---|---|---|
phosphonoacetatea | 0.27 ± 0.1 | 0.060 ± 0.009 | 5 × 103 |
phosphonoacetatea (30 °C) | 0.67 ± 0.1 | 0.015 ± 0.001 | 4 × 104 |
p-nitrophenylphosphateb | 0.22 ± 0.1 | 14 ± 0.2 | 2 × 101 |
2-phosphoglyceratea,c | 4 × 10−5 | ------ | ------ |
3-phosphoglycerola,c | 4 × 10−5 | ------ | ------ |
p-nitrophenylsulfateb | ~2 × 10−7 | ~ 10 | ~2 × 10−4 |
ATPa | 2 ×10−4 | 1 | 2 × 10−1 |
phosphonopyruvatea | NAd | ------ | ------ |
phosphonoacetaldehydea | 0.027 ± 0.01 | 0.33 ± 0.01 | 8 × 101 |
fosfomycina,c | NAd | ------ | ------ |
bis-p-nitrophenylphosphateb,c | NAd | ------ | ------ |
The reaction buffer was 50 mM K+ADA (pH 7.0).
The reaction buffer was 50 mM K+TRICINE (pH 8.0).
Tested at a concentration of 2 mM. For 2-phosphoglycerate and 3-phosphoglycerol the ratio of the initial velocity and the enzyme concentration is used to approximates the kcat value.
No activity (NA) was observed within the detection limit of ~ 1 × 10−7 s−1.