Table 1 Comparison of the enzyme kinetics from MtDXPS and ΔMtDXPS.

From: First crystal structures of 1-deoxy-d-xylulose 5-phosphate synthase (DXPS) from Mycobacterium tuberculosis indicate a distinct mechanism of intermediate stabilization

Enzyme

Pyruvate

D-GAP

MtDXPS

5 µmol/L

Km: 85 ± 8 µM

kcat: 4.5 ± 0.1 × 10–3 s-1

Km: 75 ± 7 µM

kcat: 3.9 ± 0.7 × 10–3 s-1

ΔMtDXPS

2 µmol/L

Km: 125 ± 13 µM

kcat: 17.3 ± 0.4 × 10–3 s-1

Km: 112 ± 11 µM

kcat: 10.0 ± 0.3 × 10–3 s-1

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