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. 2015 Aug 5;6:591. doi: 10.3389/fpls.2015.00591

Table 2.

Properties of rice P5C dehydrogenase.

Denatured molecular mass (by SDS-PAGE) 58.2 ± 1.3 kDa
Native molecular mass (by gel permeation) 259 ± 14 kDa
Isoelectric point 5.60 ± 0.05
pH optimum 6.72
Temperature optimum 46 ± 1°C
Activation energy 54.6 ± 3.7 kjoules mol−1
Vmax (NAD+) 196.9 ± 2.1 nkat (mg protein)−1
Vmax (P5C,with NAD+ as the co-substrate) 207.7 ± 3.3 nkat (mg protein)−1
Vmax (NADP+) 49.2 ± 1.7 nkat (mg protein)−1
Vmax (P5C,with NADP+ as the co-substrate) 51.0 ± 1.0 nkat (mg protein)−1
Kcat (NAD+) 12 s−1
Kcat (NADP+) 3 s−1
KM(app) for L-P5C (NAD+) 358 ± 14 μM
KM(app) for L-P5C (NADP+) 265 ± 13μM
KM(app) for NAD+ 644 ± 30 μM
KM(app) for NADP+ 4695 ± 462 μM