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. 2016 Nov 19;6(2):e00419. doi: 10.1002/mbo3.419

Table 3.

Kinetic parameters of the studied NADP‐GDHs

Enzyme pH 7.5 pH 5.8
k cat (s−1) K m‐α‐KG (mmol/L) n H‐ α‐KG K m‐NADPH (μmol/L) n H‐NADPH K m‐NH4+ (mmol/L) n H‐NH4+ k cat (s−1) K m‐ α‐KG (mmol/L) n H‐ α‐KG
ScGdh1 13 0.37 45 8.6 12 0.31
ScGdh3 14 0.4 42 6.9 13 S 0.5=1.48 2.4
LkGdh1 20 0.46 46 7.4 10 0.34
KlGdh1 21 S 0.5=3.61 4.4 S 0.5=39 1.8 S 0.5=21.4 2.7 6 S 0.5=1.95 4

Data were fitted to the Michaelis–Menten equation except for the ScGdh3 isoform at pH 5.8 and the KlGdh1 enzyme which were fitted to the Hill equation. Standard errors for the fitted parameters at pH 7.5 were lower than 8% and, at pH 5.8, lower than 16%. For all the fitting analyses, the R 2 value was higher than 0.982.