. 2012 Oct 29;109(47):19474–19479. doi: 10.1073/pnas.1210993109

Table 2.

Kinetic properties of Rubisco purified from wild type and pyrenoid-restored Rubisco mutant (helix AB)

Enzyme	V_c^*, µmol⋅mg⁻¹⋅h⁻¹	K_c^*, µM CO₂	K_o^*^†, µM O₂	V_c/K_c^‡	K_o/K_c^‡	V_c/V_o^‡	Ω (V_cK_o/V_oK_c)^‡
Wild type	110 ± 9	30 ± 2	523 ± 18	3.7	17	3.5	61 ± 2
Helix AB	13 ± 3	35 ± 3	299 ± 59	0.4	7	7.7	54 ± 2

Carboxylation (c) and oxygenation (o) kinetic properties of Rubisco purified from spinach hybrid have been determined by the authors before (mutant SSSO in ref. 21): V_c = 97, K_c = 34, K_o = 539, V_c/K_c = 2.9; K_o/K_c = 16; V_c/V_o = 4.1; Ω = 65. K (in micromolar concentration) is the K_m and V (in micromolar hour⁻¹ milligram⁻¹) is the V_max of purified and activated Rubisco.

*Values are the means ± 1 SD of three biological replicates.

^†The Michaelis–Menten constant is measured as the O₂ inhibition constant for the carboxylation reaction (K_io) and is assumed to equal K_o (also noted K_mO2).

^‡Calculated values.