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. 2019 Nov 5;60(1):87–95. doi: 10.1007/s12088-019-00834-w

Table 3.

Kinetic constants for P. pini GDH enzyme. Initial rates were measured under conditions as described in Sect. 2.8. Results are expressed as mean ± SD

Km (mM) Vmax (μmol/min/mg) kcat (s−1)a kcat/Km
NAD 0.25 ± 0.01 247.5 ± 3.5 115.4 ± 2.5 462.1 ± 16.3
NADP 2.16 ± 0.2 333 ± 5.7 155.4 ± 3.9 143.5 ± 16.6
Glucose (with NAD) 26.75 ± 1.1

akcat values were calculated for single subunit of the enzyme