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. Author manuscript; available in PMC: 2008 Aug 12.
Published in final edited form as: Biochemistry. 2006 Jul 25;45(29):8988–8999. doi: 10.1021/bi0606602

Table 1.

Steady-State Kinetic Parameters for M. tuberculosis IPMSa

Fixed Substrate Variable Substrate kcat (s−1) Km (μM) kcat/Km (s−1 M−1) (×10−2)
AcCoA α—KIV 3.5 ± 0.1 12 ± 1 34000 ± 260
AcCoA α—KV 7.0 ± 1.3 410 ± 180 5900 ± 80
AcCoA α—KB 10.7 ± 0.4 860 ± 160 8000 ± 25
AcCoA PY 6.1 ± 0.5 9500 ± 1680 16 ± 1
α—KIV AcCoA 2.1 ± 0.1 136 ± 5 150 ± 9
α—KV AcCoA 5.0 ± 0.2 279 ± 31 180 ± 20
α—KB AcCoA 7.6 ± 0.1 57 ± 2 1300 ± 49
PY AcCoAb 4.5 ± 0.3 74 ± 13 610 ± 120
a

At pH 7.4 and 25°C. The following concentrations of fixed co-substrate were used: 1 mM AcCoA, 250 μM α—KIV, 4 mM α—KV, 10 mM α—KB, and 100 mM PY.

b

Saturation curves displaying apparent linear substrate inhibition were fitted to eq. 2. The Ki for α—KV at a fixed saturating concentration of AcCoA was 10.1 ± 4.4 mM, and the Ki for AcCoA in the presence of a fixed saturating concentration of pyruvate was 4.0 ± 1.3 mM.