Catalytic variation at 25°C among the Rubisco superfamily

Range Table - link
Organism Various
Reference Robert H. Wilson, Spencer M. Whitney, Improving CO2 Fixation by Enhancing Rubisco Performance, 15 February 2017, Directed Enzyme Evolution: Advances and Applications, pp 101-126 p.105 table 4.1
Primary Source See refs beneath table
Comments P.105 top paragraph: "The complexity of this catalytic chemistry, that is compounded by the inability of Rubisco to bind either gas substrate, has posed a significant challenge to both nature and scientific research in identifying solutions for improving Rubisco performance [ref 53]. Nevertheless, the large natural diversity in the catalytic properties of Rubisco (Table 4.1) confirms evolutionary adaptation of the enzyme. For example, Rubisco from organisms with CO2 concentrating mechanisms (CCM) that elevate CO2 concentrations around the enzyme typically have higher CO2 fixation rates (kcatC) but lower CO2 affinities (i.e. a higher Km for CO2, KC) [primary source 67], although this does not appear to be the case for diatom (nongreen microalgae) Rubisco (Table 4.1) [primary source 92]."
Entered by Uri M
ID 113687