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. 2017 Jun 22;34(2):107–113. doi: 10.5511/plantbiotechnology.17.0326a

Table 1. Enzymatic kinetics for the sucrose degradation by the isoforms of rice sucrose synthase.

Sucrose+UDP
Isoform Phosphor-ylation Km (mM) Vmax (nmol min−1 (µg protein)−1) kcat (min−1) catalytic efficiency (min−1 mM−1)
Rsus1 219±50.6 3.23±0.25 295±33.7 1.33±0.15
+ 160±49.0 3.37±0.21 308±14.7 1.80±0.26
Rsus2 82.7±26.5 2.73±0.06 255±5.13 3.80±1.32
+ 74.7±8.62 3.83±0.47 355±44.5 4.77±0.67
Rsus3 525±54.2 1.63±0.06 149±8.39 0.29±0.01
+ 384±93.0 1.67±0.20 151±18.0 0.41±0.06
Sucrose+ADP
Isoform Phosphor-ylation Km (mM) Vmax (nmol min−1 (µg protein)−1) kcat (min−1) catalytic efficiency (min−1 mM−1)
Rsus1 1799±358 1.47±0.15 129±14.2 0.08±0.01
+ 1571±92.1 1.93±0.21 170±21.1 0.12±0.03
Rsus2 896±165 1.77±0.38 163±40.9 0.19±0.09
+ 781±94.8 2.03±0.51 185±47.6 0.24±0.09
Rsus3 2085±89.6 1.40±0.17 128±19.2 0.06±0.01
+ 1467±92.6 1.55±0.35 131±31.8 0.10±0.02

Kinetic parameters, Km and Vmax, were evaluated by Lineweaver–Burk plots (Supplementary Figure 2), which were determined on the reactions for sucrose degradation (see Figure 2). Values were determined on the correlation between amounts of fructose generated and sucrose with UDP or ADP as substrates. kcat was estimated as Vmax/enzyme content. Catalytic efficiency was evaluated as the value of kcat/Km. Each value±SD is shown (n=5).