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. Author manuscript; available in PMC: 2021 Apr 7.
Published in final edited form as: Biochemistry. 2020 Mar 18;59(13):1328–1337. doi: 10.1021/acs.biochem.0c00097

Table 1.

Steady-state kinetic parameters for Cj1427a

Enzyme Substrate kcat (s−1) Km (μM) kcat/Km (M−1 s−1)
Cj1427 GDP-d-glycero-α-d-manno-heptoseb 0.64 ± 0.02 63 ± 5 (10.2 ± 0.8) × 103
Cj1427 α-ketoglutaratec 0.55 ± 0.01 130 ± 8 (4.3 ± 0.3) × 103
a

Errors were calculated from the standard deviation of the fitting results. Reactions were monitored by UV coupled assay at 340 nm in 50 mM HEPES/KCl, pH 7.4 at 30 °C in the presence of 300 μM NADPH and 10 μM Cj1430 and Cj1428.

b

The concentration of GDP-d-glycero-α-d-manno-heptose was varied with a fixed concentration of α-ketoglutarate (1.0 mM).

c

Concentration of α-ketoglutarate was varied with a fixed concentration GDP-d-glycero-d-manno-heptose (0.5 mM).