Table 1 Kinetic characterization of M. tuberculosis branched-chain aminotransferase. The enzyme was incubated with varying concentrations of substrate and 10 mM cosubstrate, as described in the Methods section.
From: Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis
Substrate | Cosubstrate | Apparent Km (mM) | Apparent Vmax (μmol/min/mg protein) |
|---|---|---|---|
Leu | KMTB | 2.50 ± 0.90 | 3.65 ± 0.43 |
Val | KMTB | 1.77 ± 0.86 | 2.58 ± 0.41 |
Ile | KMTB | 2.85 ± 0.56 | 4.28 ± 0.32 |
Glu | KMTB | 9.53 ± 3.43 | 5.70 ± 1.20 |
Phe | KMTB | 7.44 ± 1.40 | 2.17 ± 0.22 |
KMTB | Leu | 4.20 ± 1.79 | 4.22 ± 0.72 |
Leu | KG | 6.02 ± 0.94 | 13.44 ± 0.84 |
Val | KG | 5.79 ± 0.99 | 11.82 ± 0.80 |
Ile | KG | 6.16 ± 1.14 | 14.35 ± 1.08 |
KG | Leu | 6.95 ± 1.44 | 12.80 ± 1.12 |