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. 2019 May 15;5(6):939–948. doi: 10.1021/acscentsci.9b00228

Table 1. Experimental Reports of Enhanced Enzyme Diffusion.

enzyme native form Mw (kDa) kcat (s–1) D0 (μm2/s) De,max (μm2/s) D/D0 method ref
urease (jack bean) hexamer 544 2 × 104 31.8 40.6 1.28 FCS (45)
catalase (bovine liver) tetramer 250 5.8 × 104 61a 79 1.3 FCS (5)
alkaline phosphatase from bovine intestinal mucosa dimer 160 1.4 × 104 NMb NM 1.8 FCS (5)
acetylcholinesterase (E. electricus) four different forms 430 (8S), 780 (14S), 1100 (18S), 280 (11S) NM 22 27 1.23 STED-FCS (6)
hexokinase (Saccharomyces cerevisiae) dimer 110 200 72.4c 106 1.46 FCS (3536)
aldolase (rabbit muscle) tetramer 158 5 42.6 56 1.31 FCS (25)
α subunit of F1-ATPase monomer 58.7   56.4 64.5 1.14 light scattering (7)
F1-ATPase (Escherichia coli) α3β3γδε complex 381d38 ∼100d39 33 41 1.24 FCS (40)
a

The diffusion coefficient of catalase was measured to be 41 μm2/s by Sumner.41

b

NM: not mentioned.

c

The diffusion coefficients of hexokinase monomer and dimer were measured to be 74.6 and 56.4 μm2/s, respectively.42

d

Data from a different reference.