Table 1 in How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?

Table 1 Kinetic parameters of P. crispum SDH. V max - maximal reaction rate of enzyme reaction, K - Michaelis constant of the specific substrate, K ′ -apparent m m Michaelis constant at a given concentration of the second substrate), KSS - inhibition constant at an excess substrate concentration, KA - dissociation constant of the enzyme – substrate complex, ♣ for technical reasons (absorbance above 3 or excess substrate inhibition), this parameter could not be determined. Kinetic constants were calculated as an average of values from at least 3 experiments performed in doublets, S. D. are shown.
Direction of the reaction catalyzed bySDHSA → DHSDHS → SApH optimum9.5–107–8.5V [μmol.min 1.mg 1] for SA (DHS) max1.340.29V [μmol.min 1.mg 1] for NADP(H) max1.320.28K m for SA (DHS) [mM]0.71 ± 0.13♣K m for NADP(H) [mM]0.47 ± 0.16♣K ′ for SA (with 0.2 mM NADP) [mM] m0.16 ± 0.01–K ′ for DHS (with 0.4 mM NADPH) [mM] m–0.23 ± 0.03K ′ for NADP (with 3 mM SA) [mM] m0.054 ± 0.011–K ′ for NADPH (with 2 mM DHS) [mM] m–0.016 ± 0.03KSS for SA (DHS) [mM]–0.12 ± 0.07KA [mM]0.030 ± 0.0080.25 ± 0.13