Table 2.
Rubisco source | kcatC | kcatO | KMCO2 | KMO2 | KMRuBP | Substrate specificity factor | Carboxylation efficiency | References |
(1/s) | (1/s) | (μM) | (μM) | (μM) | (SC/O) | (kcatC/KMCO2) (1/s/μM) | ||
Tobacco | 3.40 | 1.14 | 10.7 | 295 | 18.0 | 82 | 0.318 | (67) |
Synechococcus | 14.4 | 1.22* | 172 | 585* | 69.9 | 40 | 0.084 | (36, 40) |
Cyanobium | 9.40 | 1.42† | 169 | 1,400† | 40.0 | 55 | 0.056 | (15, 41) |
Ancestral F1A | 4.77 | 1.42 | 113 | 2,010 | 40.0‡ | 60 | 0.042 | (15, 41) |
Ancestral F1B | 4.72 | 0.50 | 120 | 641 | 69.9‡ | 50 | 0.039 | (15, 36) |
Chlamydomonas | 2.91 | 0.61 | 33.0 | 422 | 19.0§ | 61 | 0.088 | (42, 43) |
The kcatO and KMO2 for Synechococcus Rubisco are from Occhialini, Lin, Andralojc, Hanson, and Parry (40).
The kcatO of the Cyanobium enzyme was estimated using the Prochlorococcus KMO2 (15), and the published values of kcatC, KMCO2, and SC/O for Cyanobium (41) using kcatO = [(kcatC × KMO2)/SC/O]/KMCO2.
KMRuBP values for Ancestral F1A and F1B enzymes are those of Cyanobium and Synechococcus, respectively, from the references highlighted.