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. 2016 Feb 10;7:10619. doi: 10.1038/ncomms10619

Table 1. Enzyme kinetic data for each individual enzyme encapsulated inside a DNA full-cage in comparison with the values for the free enzymes in solution.

Enzyme pI Molecular weight Substrate Free enzymes
Encapsulated enzymes
        Km (μM) kcat (s−1) Km (μM) kcat (s−1)
GOx 4.2 160 kDa Glucose 6,200±900 240±10 3,000±600 1,300±50
HRP 8.8 44 kDa H2O2 2.3±0.5 32±1 4.3±0.6 290±5
      ABTS 2,600±400 59±5 2,500±200 560±20
G6pDH 4.3 100 kDa Glucose-6-phosphate 220±20 130±3 310±30 460±10
      NAD+ 510±50 100±3 590±40 480±10
MDH 10.0 70 kDa NADH 180±50 51±5 270±50 460±30
LDH 5.0 140 kDa NADH 7.2±1.3 46±2 17.0±1.5 190±5
β-Gal 4.1 465 kDa RBG 58.7±16.0 8.5±0.6* 95.5±18.9 1.6±0.1*

ABTS, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid); GOx, glucose oxidase; G6pDH, glucose-6-phosphate dehydrogenase; HRP, horseradish peroxidase; LDH, lactic dehydrogenase; MDH, malic dehydrogenase; pI, isoelectric point.

The Michaelis–Menten plots of each enzyme and the conditions of the enzyme activity measurements can be found in the Supplementary Figs. The pI values of the enzymes were obtained from brenda-enzymes.org (refs 65, 66, 67, 68).

*kcat values for β-Gal groups were not calibrated.